E-175 Search Results


cac1-derived peptides cac1c (e 175 sasssvkawmtetllvqna 194)  (GenScript corporation)
90
GenScript corporation cac1-derived peptides cac1c (e 175 sasssvkawmtetllvqna 194)
(A) Ribbon model of the three dimensional structure of the CTD dimer . The two monomers are represented in green or blue. Helix 9 is labelled. (B) Sequence of CAC1 including helix 9 residues, and of designed CAC1-derived peptides. (C) Variation in <λ> of the fluorescence emission spectrum of wild-type dimeric CTD with the concentration of added <t>CAC1C.</t> Fitting to a 1∶1 binding isotherm as described is indicated by a thin line. A similar affinity constant was obtained when the fluorescence intensity at 315 nm instead of <λ> was represented. (D) Variation in fluorescence emission intensity at 315 nm of wild-type dimeric CTD with the concentration of added CAC1M.
Cac1 Derived Peptides Cac1c (E 175 Sasssvkawmtetllvqna 194), supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/cac1-derived peptides cac1c (e 175 sasssvkawmtetllvqna 194)/product/GenScript corporation
Average 90 stars, based on 1 article reviews
cac1-derived peptides cac1c (e 175 sasssvkawmtetllvqna 194) - by Bioz Stars, 2026-03
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phs e-175–2010  (psychology software tools)
90
psychology software tools phs e-175–2010
(A) Ribbon model of the three dimensional structure of the CTD dimer . The two monomers are represented in green or blue. Helix 9 is labelled. (B) Sequence of CAC1 including helix 9 residues, and of designed CAC1-derived peptides. (C) Variation in <λ> of the fluorescence emission spectrum of wild-type dimeric CTD with the concentration of added <t>CAC1C.</t> Fitting to a 1∶1 binding isotherm as described is indicated by a thin line. A similar affinity constant was obtained when the fluorescence intensity at 315 nm instead of <λ> was represented. (D) Variation in fluorescence emission intensity at 315 nm of wild-type dimeric CTD with the concentration of added CAC1M.
Phs E 175–2010, supplied by psychology software tools, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/phs e-175–2010/product/psychology software tools
Average 90 stars, based on 1 article reviews
phs e-175–2010 - by Bioz Stars, 2026-03
90/100 stars
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e175 1/0 1z  (Nitto Boseki Co Ltd)
90
Nitto Boseki Co Ltd e175 1/0 1z
(A) Ribbon model of the three dimensional structure of the CTD dimer . The two monomers are represented in green or blue. Helix 9 is labelled. (B) Sequence of CAC1 including helix 9 residues, and of designed CAC1-derived peptides. (C) Variation in <λ> of the fluorescence emission spectrum of wild-type dimeric CTD with the concentration of added <t>CAC1C.</t> Fitting to a 1∶1 binding isotherm as described is indicated by a thin line. A similar affinity constant was obtained when the fluorescence intensity at 315 nm instead of <λ> was represented. (D) Variation in fluorescence emission intensity at 315 nm of wild-type dimeric CTD with the concentration of added CAC1M.
E175 1/0 1z, supplied by Nitto Boseki Co Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/e175 1/0 1z/product/Nitto Boseki Co Ltd
Average 90 stars, based on 1 article reviews
e175 1/0 1z - by Bioz Stars, 2026-03
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l e 175  (Schill Seilacher GmbH)
90
Schill Seilacher GmbH l e 175
(A) Ribbon model of the three dimensional structure of the CTD dimer . The two monomers are represented in green or blue. Helix 9 is labelled. (B) Sequence of CAC1 including helix 9 residues, and of designed CAC1-derived peptides. (C) Variation in <λ> of the fluorescence emission spectrum of wild-type dimeric CTD with the concentration of added <t>CAC1C.</t> Fitting to a 1∶1 binding isotherm as described is indicated by a thin line. A similar affinity constant was obtained when the fluorescence intensity at 315 nm instead of <λ> was represented. (D) Variation in fluorescence emission intensity at 315 nm of wild-type dimeric CTD with the concentration of added CAC1M.
L E 175, supplied by Schill Seilacher GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/l e 175/product/Schill Seilacher GmbH
Average 90 stars, based on 1 article reviews
l e 175 - by Bioz Stars, 2026-03
90/100 stars
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Image Search Results


(A) Ribbon model of the three dimensional structure of the CTD dimer . The two monomers are represented in green or blue. Helix 9 is labelled. (B) Sequence of CAC1 including helix 9 residues, and of designed CAC1-derived peptides. (C) Variation in <λ> of the fluorescence emission spectrum of wild-type dimeric CTD with the concentration of added CAC1C. Fitting to a 1∶1 binding isotherm as described is indicated by a thin line. A similar affinity constant was obtained when the fluorescence intensity at 315 nm instead of <λ> was represented. (D) Variation in fluorescence emission intensity at 315 nm of wild-type dimeric CTD with the concentration of added CAC1M.

Journal: PLoS ONE

Article Title: Rationally Designed Interfacial Peptides Are Efficient In Vitro Inhibitors of HIV-1 Capsid Assembly with Antiviral Activity

doi: 10.1371/journal.pone.0023877

Figure Lengend Snippet: (A) Ribbon model of the three dimensional structure of the CTD dimer . The two monomers are represented in green or blue. Helix 9 is labelled. (B) Sequence of CAC1 including helix 9 residues, and of designed CAC1-derived peptides. (C) Variation in <λ> of the fluorescence emission spectrum of wild-type dimeric CTD with the concentration of added CAC1C. Fitting to a 1∶1 binding isotherm as described is indicated by a thin line. A similar affinity constant was obtained when the fluorescence intensity at 315 nm instead of <λ> was represented. (D) Variation in fluorescence emission intensity at 315 nm of wild-type dimeric CTD with the concentration of added CAC1M.

Article Snippet: CAC1 (E 175 QASQEVKNWMTETLLVQNA 194 ) , CAC1-derived peptides CAC1C (E 175 SASSSVKAWMTETLLVQNA 194 ),CAC1M(SE 175 SAASSVKAWMTETLLVAN 193 TSS) and a control, non CTD-binding, thioredoxin binding peptide (ESLPDYGDDSDDNTLGTEEQRSIVNVSQ) derived from pea chloroplast fructose-1,6-biphosphatase (Fbase), were synthesized and purified by Genscript, NJ, USA.

Techniques: Sequencing, Derivative Assay, Fluorescence, Concentration Assay, Binding Assay

Parameters for self-association and CTD binding of CAC1-derived peptides <xref ref-type= a ." width="100%" height="100%">

Journal: PLoS ONE

Article Title: Rationally Designed Interfacial Peptides Are Efficient In Vitro Inhibitors of HIV-1 Capsid Assembly with Antiviral Activity

doi: 10.1371/journal.pone.0023877

Figure Lengend Snippet: Parameters for self-association and CTD binding of CAC1-derived peptides a .

Article Snippet: CAC1 (E 175 QASQEVKNWMTETLLVQNA 194 ) , CAC1-derived peptides CAC1C (E 175 SASSSVKAWMTETLLVQNA 194 ),CAC1M(SE 175 SAASSVKAWMTETLLVAN 193 TSS) and a control, non CTD-binding, thioredoxin binding peptide (ESLPDYGDDSDDNTLGTEEQRSIVNVSQ) derived from pea chloroplast fructose-1,6-biphosphatase (Fbase), were synthesized and purified by Genscript, NJ, USA.

Techniques: Binding Assay

(A) Mapping on the CTD sequence of the residues affected by peptide binding. Red, green or blue circles denote residues affected by binding of CAC1, CAC1C or CAC1M, respectively. (B, C) Surface model of one of the monomeric subunits in the CTD dimer. In (B) the residues involved in the CTD dimerization interface are coloured magenta. The ribbon tracing of the helix 9 main chain is superimposed. In (C) the residues affected by binding of the peptides are colored as follows: bright red, residues affected by binding of any peptide; dark red, orange or brown, residues affected by binding of CAC1 and CAC1C, CAC1 and CAC1M, or CAC1C and CAC1M, respectively.

Journal: PLoS ONE

Article Title: Rationally Designed Interfacial Peptides Are Efficient In Vitro Inhibitors of HIV-1 Capsid Assembly with Antiviral Activity

doi: 10.1371/journal.pone.0023877

Figure Lengend Snippet: (A) Mapping on the CTD sequence of the residues affected by peptide binding. Red, green or blue circles denote residues affected by binding of CAC1, CAC1C or CAC1M, respectively. (B, C) Surface model of one of the monomeric subunits in the CTD dimer. In (B) the residues involved in the CTD dimerization interface are coloured magenta. The ribbon tracing of the helix 9 main chain is superimposed. In (C) the residues affected by binding of the peptides are colored as follows: bright red, residues affected by binding of any peptide; dark red, orange or brown, residues affected by binding of CAC1 and CAC1C, CAC1 and CAC1M, or CAC1C and CAC1M, respectively.

Article Snippet: CAC1 (E 175 QASQEVKNWMTETLLVQNA 194 ) , CAC1-derived peptides CAC1C (E 175 SASSSVKAWMTETLLVQNA 194 ),CAC1M(SE 175 SAASSVKAWMTETLLVAN 193 TSS) and a control, non CTD-binding, thioredoxin binding peptide (ESLPDYGDDSDDNTLGTEEQRSIVNVSQ) derived from pea chloroplast fructose-1,6-biphosphatase (Fbase), were synthesized and purified by Genscript, NJ, USA.

Techniques: Sequencing, Binding Assay