nanoelectrospray ion source Search Results


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  • 99
    Thermo Fisher nanoelectrospray ion max source
    Nanoelectrospray Ion Max Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nanoelectrospray ion max source/product/Thermo Fisher
    Average 99 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
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    99
    Thermo Fisher nanoelectrospray ion source
    Nanoelectrospray Ion Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1529 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nanoelectrospray ion source/product/Thermo Fisher
    Average 99 stars, based on 1529 article reviews
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    nanoelectrospray ion source - by Bioz Stars, 2020-04
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    97
    New Objective Inc nanoelectrospray ion source
    Nanoelectrospray Ion Source, supplied by New Objective Inc, used in various techniques. Bioz Stars score: 97/100, based on 188 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 97 stars, based on 188 article reviews
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    93
    SCIEX nanoelectrospray ion source
    Nanoelectrospray Ion Source, supplied by SCIEX, used in various techniques. Bioz Stars score: 93/100, based on 85 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nanoelectrospray ion source/product/SCIEX
    Average 93 stars, based on 85 article reviews
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    nanoelectrospray ion source - by Bioz Stars, 2020-04
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    91
    Michrom nanoelectrospray ion source
    Nanoelectrospray Ion Source, supplied by Michrom, used in various techniques. Bioz Stars score: 91/100, based on 35 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nanoelectrospray ion source/product/Michrom
    Average 91 stars, based on 35 article reviews
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    nanoelectrospray ion source - by Bioz Stars, 2020-04
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    94
    Waters Corporation nanoelectrospray ion source
    Nanoelectrospray Ion Source, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 94/100, based on 62 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nanoelectrospray ion source/product/Waters Corporation
    Average 94 stars, based on 62 article reviews
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    nanoelectrospray ion source - by Bioz Stars, 2020-04
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    90
    Bruker Corporation nanoelectrospray ion source
    Nanoelectrospray Ion Source, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 90/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nanoelectrospray ion source/product/Bruker Corporation
    Average 90 stars, based on 20 article reviews
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    88
    MDS Proteomics nanoelectrospray ion source
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
    Nanoelectrospray Ion Source, supplied by MDS Proteomics, used in various techniques. Bioz Stars score: 88/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nanoelectrospray ion source/product/MDS Proteomics
    Average 88 stars, based on 15 article reviews
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    nanoelectrospray ion source - by Bioz Stars, 2020-04
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    94
    Thermo Fisher nanoelectropsray ion source
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
    Nanoelectropsray Ion Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nanoelectropsray ion source/product/Thermo Fisher
    Average 94 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    nanoelectropsray ion source - by Bioz Stars, 2020-04
    94/100 stars
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    92
    Thermo Fisher nanoeletrospray ion source
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
    Nanoeletrospray Ion Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nanoeletrospray ion source/product/Thermo Fisher
    Average 92 stars, based on 5 article reviews
    Price from $9.99 to $1999.99
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    88
    Thermo Fisher nanoelectrospay ion source
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
    Nanoelectrospay Ion Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nanoelectrospay ion source/product/Thermo Fisher
    Average 88 stars, based on 11 article reviews
    Price from $9.99 to $1999.99
    nanoelectrospay ion source - by Bioz Stars, 2020-04
    88/100 stars
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    94
    Thermo Fisher proxeon nanoelectrospray ion source
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
    Proxeon Nanoelectrospray Ion Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 104 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/proxeon nanoelectrospray ion source/product/Thermo Fisher
    Average 94 stars, based on 104 article reviews
    Price from $9.99 to $1999.99
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    92
    Advion chipmatetm nanoelectrospray ion source
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
    Chipmatetm Nanoelectrospray Ion Source, supplied by Advion, used in various techniques. Bioz Stars score: 92/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/chipmatetm nanoelectrospray ion source/product/Advion
    Average 92 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    chipmatetm nanoelectrospray ion source - by Bioz Stars, 2020-04
    92/100 stars
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    92
    Thermo Fisher easy1000 nanoelectrospray ion source
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
    Easy1000 Nanoelectrospray Ion Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/easy1000 nanoelectrospray ion source/product/Thermo Fisher
    Average 92 stars, based on 5 article reviews
    Price from $9.99 to $1999.99
    easy1000 nanoelectrospray ion source - by Bioz Stars, 2020-04
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    91
    Michrom thermo captivespray nanoelectrospray ion source
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
    Thermo Captivespray Nanoelectrospray Ion Source, supplied by Michrom, used in various techniques. Bioz Stars score: 91/100, based on 45 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/thermo captivespray nanoelectrospray ion source/product/Michrom
    Average 91 stars, based on 45 article reviews
    Price from $9.99 to $1999.99
    thermo captivespray nanoelectrospray ion source - by Bioz Stars, 2020-04
    91/100 stars
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    93
    Thermo Fisher easy spray nanoelectrospray ion source
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
    Easy Spray Nanoelectrospray Ion Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 63 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/easy spray nanoelectrospray ion source/product/Thermo Fisher
    Average 93 stars, based on 63 article reviews
    Price from $9.99 to $1999.99
    easy spray nanoelectrospray ion source - by Bioz Stars, 2020-04
    93/100 stars
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    90
    Advion triversa nanomate nanoelectrospray ion source
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
    Triversa Nanomate Nanoelectrospray Ion Source, supplied by Advion, used in various techniques. Bioz Stars score: 90/100, based on 29 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/triversa nanomate nanoelectrospray ion source/product/Advion
    Average 90 stars, based on 29 article reviews
    Price from $9.99 to $1999.99
    triversa nanomate nanoelectrospray ion source - by Bioz Stars, 2020-04
    90/100 stars
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    88
    Thermo Fisher proxeon biosystems nanoelectrospray ion source
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
    Proxeon Biosystems Nanoelectrospray Ion Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/proxeon biosystems nanoelectrospray ion source/product/Thermo Fisher
    Average 88 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    proxeon biosystems nanoelectrospray ion source - by Bioz Stars, 2020-04
    88/100 stars
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    87
    Advion triversa nanomate nanoelectrospry ion source
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
    Triversa Nanomate Nanoelectrospry Ion Source, supplied by Advion, used in various techniques. Bioz Stars score: 87/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/triversa nanomate nanoelectrospry ion source/product/Advion
    Average 87 stars, based on 11 article reviews
    Price from $9.99 to $1999.99
    triversa nanomate nanoelectrospry ion source - by Bioz Stars, 2020-04
    87/100 stars
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    92
    Thermo Fisher nanoelectrospray ion source easyspray thermo
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
    Nanoelectrospray Ion Source Easyspray Thermo, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nanoelectrospray ion source easyspray thermo/product/Thermo Fisher
    Average 92 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    nanoelectrospray ion source easyspray thermo - by Bioz Stars, 2020-04
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    95
    Fisher Scientific nanoelectrospray ion source
    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
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    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
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    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
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    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
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    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
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    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
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    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
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    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
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    Ideication of the UV cross-linked amino acid residue in SSB by <t>nanoelectrospray</t> tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.
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    Image Search Results


    Ideication of the UV cross-linked amino acid residue in SSB by nanoelectrospray tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.

    Journal: Protein Science : A Publication of the Protein Society

    Article Title: Mass spectrometric analysis of a UV-cross-linked protein-DNA complex: Tryptophans 54 and 88 of E. coli SSB cross-link to DNA

    doi:

    Figure Lengend Snippet: Ideication of the UV cross-linked amino acid residue in SSB by nanoelectrospray tandem mass spectrometry of the peptide–DNA heteroconjugate. ( A ) Nanoelectrospray mass spectrum obtained from the Oligo R3 eluate after tryptic digest, IMAC purification, and phosphodiesterase I digest. The major ion signal is attributable to a triply charged species at m/z 779.62. ( B ) First MS/MS fragmentation regime: product ion spectrum of the triply charged species at m/z 779.62 at a Q 0 setting of 40 V (about 60 eV collision energy in LRF). The major fragments corresponding to the fragmentation of a trinucleotide with the sequence TpGpX are labeled. The fragments corresponding to the loss of the former 5-iodouracil are marked with triangles. No peptide backbone cleavage products are observable. ( C ) Second MS/MS fragmentation regime: product ion spectrum of the same species at a Q 0 setting of 60 V (about 120 eV collision energy in LRF). The region above m/z 300 is enlarged 46-fold showing fragments deriving from the cleavages of the amide bond. The fragment ions y 8 and y 9 unambiguously demonstrate that W88 was cross-linked to the DNA. Sequence specific fragment ions are labeled. ( D ) in bold face; amino acid one-letter code underlined in bold face. The lower part shows the fragmentation of the peptide at a collision energy of about 120 eV. The peptide fragment ions are labeled according to Biemann (1988). ( E ) Product ion spectrum of the triply charged peptide–trinucleotide heteroconjugate at m/z 615.5, revealing Trp-54 to be the second UV-cross-linked amino acid residue.

    Article Snippet: Analytical properties of the nanoelectrospray ion source.

    Techniques: Mass Spectrometry, Purification, Sequencing, Labeling