Design of peptide inhibitors that bind the bZIP domain of Epstein-Barr virus protein BZLF1
about
Designing specific protein-protein interactions using computation, experimental library screening, or integrated methodsData-driven prediction and design of bZIP coiled-coil interactions.Combined computational design of a zinc-binding site and a protein-protein interaction: one open zinc coordination site was not a robust hotspot for de novo ubiquitin bindingStrategies to control the binding mode of de novo designed protein interactions.A set of computationally designed orthogonal antiparallel homodimers that expands the synthetic coiled-coil toolkit.Designing helical peptide inhibitors of protein-protein interactionsIncreasing the affinity of selective bZIP-binding peptides through surface residue redesign.The d'--d--d' vertical triad is less discriminating than the a'--a--a' vertical triad in the antiparallel coiled-coil dimer motif.
P2860
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P2860
Design of peptide inhibitors that bind the bZIP domain of Epstein-Barr virus protein BZLF1
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Design of peptide inhibitors t ...... stein-Barr virus protein BZLF1
@en
type
label
Design of peptide inhibitors t ...... stein-Barr virus protein BZLF1
@en
prefLabel
Design of peptide inhibitors t ...... stein-Barr virus protein BZLF1
@en
P2860
P1476
Design of peptide inhibitors t ...... stein-Barr virus protein BZLF1
@en
P2093
Aaron W Reinke
T Scott Chen
P2860
P304
P356
10.1016/J.JMB.2011.02.046
P407
P577
2011-02-25T00:00:00Z