Stereochemical constraints in peptide design: Analysis of the influence of a disulfide bridge and an ?-aminoisobutyryl residue on the conformation of a hexapeptide-Reference-Cited by-同舟云学术

Stereochemical constraints in peptide design: Analysis of the influence of a disulfide bridge and an ?-aminoisobutyryl residue on the conformation of a hexapeptide

Published:1993-06 Issue:6 Volume:33 Page:865-871
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Uma K.,Kishore R.,Balaram P.

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Reference23 articles.

1. Conformational analysis of small disulfide loops. Spectroscopic and theoretical studies on a synthetic cyclic tetrapeptide containing cystine

2. Cyclic peptide disulfides. Solution and solid-state conformation of Boc-Cys-Pro-Aib-Cys-NHMe with a disulfide bridge from Cys to Cys, a disulfide-bridged peptide helix

3. Stabilization of β-turn conformations in Pro-X sequences by disulphide bridging. Synthesis and solution conformations of five cyclic cystine peptides

4. Chain reversals in model peptides: studies of cystine-containing cyclic peptides. 1. Conformational free energies of cyclization of hexapeptides of sequence Ac-Cys-X-Pro-Gly-Y-Cys-NHMe

5. Chain reversals in model peptides: studies of cystine-containing cyclic peptides II. Effects of valyl residues and possible i-to-(i + 3) attractive ionic interactions on cyclization of [Cys1], [Cys6] hexapeptides

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