Tetrad selectivity in polarity-driven switch peptides: the best turn is not always the best nucleation site
Author:
Publisher
Wiley
Subject
Organic Chemistry,Drug Discovery,Pharmacology,Molecular Biology,Molecular Medicine,General Medicine,Biochemistry,Structural Biology
Reference30 articles.
1. A conformational switch is associated with receptor affinity in peptides derived from the CD4-binding domain of gp120 from HIV I;Reed;Biochemistry,1991
2. Primary structure elements responsible for the conformational switch in the envelope glycoprotein gp120 from human immunodeficiency virus type 1: LPCR is a motif governing folding;Reed;Proc. Natl. Acad. Sci. U.S.A.,1993
3. Successful design and synthesis of a polarity-triggered beta → alpha conformational switch using the side chain interaction index (SCII) as a measure of local structural stability;Gehenn;Biochemistry,2004
4. Investigation of the structural components governing the polarity-dependent refolding of a CD4-binding peptide from gp120;Graf von Stosch;J. Mol. Biol.,1995
5. Empirical predictions of protein conformation;Chou;Annu. Rev. Biochem.,1978
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