program of the dnastar package version 7.0 Search Results


program dnastar lasergene  (DNASTAR)
99
DNASTAR program dnastar lasergene
FIG. 2. Amino acid sequence of antigenic fragments 52/3 and UL57/3 of pUL44 and pUL57, respectively, and sequence comparison by dot plot analysis. Amino acids with respect to pUL44 (p52) and pUL57 contained in recombinant antigens 52/3 and UL57/3 are given in brackets. Numbers indicate amino acid positions with respect to recombinant proteins. (A) Amino acid sequence of the carboxy-terminal part of p52 (pUL44) and the internal portion of pUL57 in HCMV recombinant antigens. Glycine-rich motifs GL, GS, GA, and GR are depicted by boxes. (B) Dot-plot comparison of 52/3 and UL57/3 using the program DNASTAR <t>Lasergene</t> (similarity, 70%; window, 10). Shading of graphs indicates the level of homology.
Program Dnastar Lasergene, supplied by DNASTAR, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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dnastar7 0 software  (DNASTAR)
99
DNASTAR dnastar7 0 software
FIG. 2. Amino acid sequence of antigenic fragments 52/3 and UL57/3 of pUL44 and pUL57, respectively, and sequence comparison by dot plot analysis. Amino acids with respect to pUL44 (p52) and pUL57 contained in recombinant antigens 52/3 and UL57/3 are given in brackets. Numbers indicate amino acid positions with respect to recombinant proteins. (A) Amino acid sequence of the carboxy-terminal part of p52 (pUL44) and the internal portion of pUL57 in HCMV recombinant antigens. Glycine-rich motifs GL, GS, GA, and GR are depicted by boxes. (B) Dot-plot comparison of 52/3 and UL57/3 using the program DNASTAR <t>Lasergene</t> (similarity, 70%; window, 10). Shading of graphs indicates the level of homology.
Dnastar7 0 Software, supplied by DNASTAR, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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editseq  (DNASTAR)
96
DNASTAR editseq
FIG. 2. Amino acid sequence of antigenic fragments 52/3 and UL57/3 of pUL44 and pUL57, respectively, and sequence comparison by dot plot analysis. Amino acids with respect to pUL44 (p52) and pUL57 contained in recombinant antigens 52/3 and UL57/3 are given in brackets. Numbers indicate amino acid positions with respect to recombinant proteins. (A) Amino acid sequence of the carboxy-terminal part of p52 (pUL44) and the internal portion of pUL57 in HCMV recombinant antigens. Glycine-rich motifs GL, GS, GA, and GR are depicted by boxes. (B) Dot-plot comparison of 52/3 and UL57/3 using the program DNASTAR <t>Lasergene</t> (similarity, 70%; window, 10). Shading of graphs indicates the level of homology.
Editseq, supplied by DNASTAR, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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arraystar 4  (DNASTAR)
95
DNASTAR arraystar 4
FIG. 2. Amino acid sequence of antigenic fragments 52/3 and UL57/3 of pUL44 and pUL57, respectively, and sequence comparison by dot plot analysis. Amino acids with respect to pUL44 (p52) and pUL57 contained in recombinant antigens 52/3 and UL57/3 are given in brackets. Numbers indicate amino acid positions with respect to recombinant proteins. (A) Amino acid sequence of the carboxy-terminal part of p52 (pUL44) and the internal portion of pUL57 in HCMV recombinant antigens. Glycine-rich motifs GL, GS, GA, and GR are depicted by boxes. (B) Dot-plot comparison of 52/3 and UL57/3 using the program DNASTAR <t>Lasergene</t> (similarity, 70%; window, 10). Shading of graphs indicates the level of homology.
Arraystar 4, supplied by DNASTAR, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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dnastar 7 0  (DNASTAR)
97
DNASTAR dnastar 7 0
FIG. 2. Amino acid sequence of antigenic fragments 52/3 and UL57/3 of pUL44 and pUL57, respectively, and sequence comparison by dot plot analysis. Amino acids with respect to pUL44 (p52) and pUL57 contained in recombinant antigens 52/3 and UL57/3 are given in brackets. Numbers indicate amino acid positions with respect to recombinant proteins. (A) Amino acid sequence of the carboxy-terminal part of p52 (pUL44) and the internal portion of pUL57 in HCMV recombinant antigens. Glycine-rich motifs GL, GS, GA, and GR are depicted by boxes. (B) Dot-plot comparison of 52/3 and UL57/3 using the program DNASTAR <t>Lasergene</t> (similarity, 70%; window, 10). Shading of graphs indicates the level of homology.
Dnastar 7 0, supplied by DNASTAR, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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integral protean 3d applicationwas  (DNASTAR)
95
DNASTAR integral protean 3d applicationwas
FIG. 2. Amino acid sequence of antigenic fragments 52/3 and UL57/3 of pUL44 and pUL57, respectively, and sequence comparison by dot plot analysis. Amino acids with respect to pUL44 (p52) and pUL57 contained in recombinant antigens 52/3 and UL57/3 are given in brackets. Numbers indicate amino acid positions with respect to recombinant proteins. (A) Amino acid sequence of the carboxy-terminal part of p52 (pUL44) and the internal portion of pUL57 in HCMV recombinant antigens. Glycine-rich motifs GL, GS, GA, and GR are depicted by boxes. (B) Dot-plot comparison of 52/3 and UL57/3 using the program DNASTAR <t>Lasergene</t> (similarity, 70%; window, 10). Shading of graphs indicates the level of homology.
Integral Protean 3d Applicationwas, supplied by DNASTAR, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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megalign pro applications  (DNASTAR)
96
DNASTAR megalign pro applications
FIG. 2. Amino acid sequence of antigenic fragments 52/3 and UL57/3 of pUL44 and pUL57, respectively, and sequence comparison by dot plot analysis. Amino acids with respect to pUL44 (p52) and pUL57 contained in recombinant antigens 52/3 and UL57/3 are given in brackets. Numbers indicate amino acid positions with respect to recombinant proteins. (A) Amino acid sequence of the carboxy-terminal part of p52 (pUL44) and the internal portion of pUL57 in HCMV recombinant antigens. Glycine-rich motifs GL, GS, GA, and GR are depicted by boxes. (B) Dot-plot comparison of 52/3 and UL57/3 using the program DNASTAR <t>Lasergene</t> (similarity, 70%; window, 10). Shading of graphs indicates the level of homology.
Megalign Pro Applications, supplied by DNASTAR, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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gphysd  (DNASTAR)
95
DNASTAR gphysd
Protein structure predictions of the variants impacting p.Cys1719 and p.Cys1721 residues. (A) Using NovaFold AI, protein structure predictions were obtained using the <t>WT</t> <t>cb-EGF-like</t> 14/TB5/cb-EGF-like 15 peptidic sequences (FBN1 WT), introducing the variations, respectively, leading to MFS (FBN1 MFS–p.(Cys1719Tyr)), <t>GPHYSD</t> [FBN1 GPHYSD-1–p.(Cys1719Trp); and FBN1 GPHYSD-2: p.(Cys1721Gly)] and WMS (FBN1 WMS–p.(Cys1721Ser)). (B) Karplus-Schulz flexibility plot, depicting the rigidity of a residue, was obtained using the corresponding protein structure predictions. A zoom on the differences is shown at the bottom right of the graph. The substitutions occur at the 67 th and 69 th residues (see supplementary data for peptidic sequences used).
Gphysd, supplied by DNASTAR, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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primerselect  (DNASTAR)
96
DNASTAR primerselect
Protein structure predictions of the variants impacting p.Cys1719 and p.Cys1721 residues. (A) Using NovaFold AI, protein structure predictions were obtained using the <t>WT</t> <t>cb-EGF-like</t> 14/TB5/cb-EGF-like 15 peptidic sequences (FBN1 WT), introducing the variations, respectively, leading to MFS (FBN1 MFS–p.(Cys1719Tyr)), <t>GPHYSD</t> [FBN1 GPHYSD-1–p.(Cys1719Trp); and FBN1 GPHYSD-2: p.(Cys1721Gly)] and WMS (FBN1 WMS–p.(Cys1721Ser)). (B) Karplus-Schulz flexibility plot, depicting the rigidity of a residue, was obtained using the corresponding protein structure predictions. A zoom on the differences is shown at the bottom right of the graph. The substitutions occur at the 67 th and 69 th residues (see supplementary data for peptidic sequences used).
Primerselect, supplied by DNASTAR, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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seqman ngen  (DNASTAR)
97
DNASTAR seqman ngen
Protein structure predictions of the variants impacting p.Cys1719 and p.Cys1721 residues. (A) Using NovaFold AI, protein structure predictions were obtained using the <t>WT</t> <t>cb-EGF-like</t> 14/TB5/cb-EGF-like 15 peptidic sequences (FBN1 WT), introducing the variations, respectively, leading to MFS (FBN1 MFS–p.(Cys1719Tyr)), <t>GPHYSD</t> [FBN1 GPHYSD-1–p.(Cys1719Trp); and FBN1 GPHYSD-2: p.(Cys1721Gly)] and WMS (FBN1 WMS–p.(Cys1721Ser)). (B) Karplus-Schulz flexibility plot, depicting the rigidity of a residue, was obtained using the corresponding protein structure predictions. A zoom on the differences is shown at the bottom right of the graph. The substitutions occur at the 67 th and 69 th residues (see supplementary data for peptidic sequences used).
Seqman Ngen, supplied by DNASTAR, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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genequest  (DNASTAR)
94
DNASTAR genequest
Protein structure predictions of the variants impacting p.Cys1719 and p.Cys1721 residues. (A) Using NovaFold AI, protein structure predictions were obtained using the <t>WT</t> <t>cb-EGF-like</t> 14/TB5/cb-EGF-like 15 peptidic sequences (FBN1 WT), introducing the variations, respectively, leading to MFS (FBN1 MFS–p.(Cys1719Tyr)), <t>GPHYSD</t> [FBN1 GPHYSD-1–p.(Cys1719Trp); and FBN1 GPHYSD-2: p.(Cys1721Gly)] and WMS (FBN1 WMS–p.(Cys1721Ser)). (B) Karplus-Schulz flexibility plot, depicting the rigidity of a residue, was obtained using the corresponding protein structure predictions. A zoom on the differences is shown at the bottom right of the graph. The substitutions occur at the 67 th and 69 th residues (see supplementary data for peptidic sequences used).
Genequest, supplied by DNASTAR, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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novadock  (DNASTAR)
93
DNASTAR novadock
Common analytical methods and software for analyzing big data in compound libraries with AI models.
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Image Search Results


FIG. 2. Amino acid sequence of antigenic fragments 52/3 and UL57/3 of pUL44 and pUL57, respectively, and sequence comparison by dot plot analysis. Amino acids with respect to pUL44 (p52) and pUL57 contained in recombinant antigens 52/3 and UL57/3 are given in brackets. Numbers indicate amino acid positions with respect to recombinant proteins. (A) Amino acid sequence of the carboxy-terminal part of p52 (pUL44) and the internal portion of pUL57 in HCMV recombinant antigens. Glycine-rich motifs GL, GS, GA, and GR are depicted by boxes. (B) Dot-plot comparison of 52/3 and UL57/3 using the program DNASTAR Lasergene (similarity, 70%; window, 10). Shading of graphs indicates the level of homology.

Journal: Clinical Diagnostic Laboratory Immunology

Article Title: Cross-Reactivity of Epstein-Barr Virus-Specific Immunoglobulin M Antibodies with Cytomegalovirus Antigens Containing Glycine Homopolymers

doi: 10.1128/cdli.8.4.747-756.2001

Figure Lengend Snippet: FIG. 2. Amino acid sequence of antigenic fragments 52/3 and UL57/3 of pUL44 and pUL57, respectively, and sequence comparison by dot plot analysis. Amino acids with respect to pUL44 (p52) and pUL57 contained in recombinant antigens 52/3 and UL57/3 are given in brackets. Numbers indicate amino acid positions with respect to recombinant proteins. (A) Amino acid sequence of the carboxy-terminal part of p52 (pUL44) and the internal portion of pUL57 in HCMV recombinant antigens. Glycine-rich motifs GL, GS, GA, and GR are depicted by boxes. (B) Dot-plot comparison of 52/3 and UL57/3 using the program DNASTAR Lasergene (similarity, 70%; window, 10). Shading of graphs indicates the level of homology.

Article Snippet: Glycine-rich motifs GL, GS, GA, and GR are depicted by boxes. (B) Dot-plot comparison of 52/3 and UL57/3 using the program DNASTAR Lasergene (similarity, 70%; window, 10).

Techniques: Sequencing, Comparison, Recombinant

Protein structure predictions of the variants impacting p.Cys1719 and p.Cys1721 residues. (A) Using NovaFold AI, protein structure predictions were obtained using the WT cb-EGF-like 14/TB5/cb-EGF-like 15 peptidic sequences (FBN1 WT), introducing the variations, respectively, leading to MFS (FBN1 MFS–p.(Cys1719Tyr)), GPHYSD [FBN1 GPHYSD-1–p.(Cys1719Trp); and FBN1 GPHYSD-2: p.(Cys1721Gly)] and WMS (FBN1 WMS–p.(Cys1721Ser)). (B) Karplus-Schulz flexibility plot, depicting the rigidity of a residue, was obtained using the corresponding protein structure predictions. A zoom on the differences is shown at the bottom right of the graph. The substitutions occur at the 67 th and 69 th residues (see supplementary data for peptidic sequences used).

Journal: Journal of Medical Genetics

Article Title: Pathogenic variants affecting the TB5 domain of the fibrillin-1 protein: not only in geleophysic/acromicric dysplasias but also in Marfan syndrome

doi: 10.1136/jmg-2023-109646

Figure Lengend Snippet: Protein structure predictions of the variants impacting p.Cys1719 and p.Cys1721 residues. (A) Using NovaFold AI, protein structure predictions were obtained using the WT cb-EGF-like 14/TB5/cb-EGF-like 15 peptidic sequences (FBN1 WT), introducing the variations, respectively, leading to MFS (FBN1 MFS–p.(Cys1719Tyr)), GPHYSD [FBN1 GPHYSD-1–p.(Cys1719Trp); and FBN1 GPHYSD-2: p.(Cys1721Gly)] and WMS (FBN1 WMS–p.(Cys1721Ser)). (B) Karplus-Schulz flexibility plot, depicting the rigidity of a residue, was obtained using the corresponding protein structure predictions. A zoom on the differences is shown at the bottom right of the graph. The substitutions occur at the 67 th and 69 th residues (see supplementary data for peptidic sequences used).

Article Snippet: Using FBN1 domain sequences of cb-EGF-like 14–TB5–cb-EGF-like 15 and introducing variants found in patients with MFS, GPHYSD and WMS (sequences used can be found in ), the domain structure predictions were performed using NovaFold AI (DNASTAR).

Techniques: Residue

Common analytical methods and software for analyzing big data in compound libraries with AI models.

Journal: BioMedicine

Article Title: Integrating natural product research laboratory with artificial intelligence: Advancements and breakthroughs in traditional medicine

doi: 10.37796/2211-8039.1475

Figure Lengend Snippet: Common analytical methods and software for analyzing big data in compound libraries with AI models.

Article Snippet: , NovaDock , https://www.dnastar.com/software/nova-protein-modeling/novaDock/ , [ ] .

Techniques: Software, Biomarker Discovery