De novo design: backbone conformational constraints in nucleating helices andβ‐hairpins
- 1 September 1999
- journal article
- review article
- Published by Wiley in Chemical Biology & Drug Design
- Vol. 54 (3) , 195-199
- https://doi.org/10.1034/j.1399-3011.1999.00119.x
Abstract
A modular approach to synthetic protein design is being developed using conformationally constrained amino acid as stereochemical directors of polypeptide chain folding. An overview of studies aimed at constructing peptide helices using alpha,alpha-dialkyated residues and beta-hairpins using D-Pro as a turn nucleator is presented. The construction of helix-helix motifs and three- and four-stranded structures has been achieved using non-protein amino acids to stabilize specific elements of secondary structuresKeywords
This publication has 48 references indexed in Scilit:
- A four stranded β-sheet structure in a designed, synthetic polypeptideChemical Communications, 1999
- Metal Ion Induced Folding of a de Novo Designed Coiled-Coil PeptideJournal of the American Chemical Society, 1998
- Construction and Design of β-SheetsAccounts of Chemical Research, 1997
- A Designed β-Hairpin PeptideBiochemical and Biophysical Research Communications, 1995
- Peptide design. Structural evaluation of potential nonhelical segments attached to helical modules.Journal of the American Chemical Society, 1995
- Native-like and structurally characterized designed α-helical bundlesCurrent Opinion in Structural Biology, 1995
- Incorporation of a Potentially Helix-Breaking D-Phe-Pro Sequence into the Center of a Right-Handed 16-Residue Peptide HelixBiochemical and Biophysical Research Communications, 1994
- α/310‐Helix transitions in α‐methylalanine homopeptides: Conformational transition pathway and potential of mean forceBiopolymers, 1994
- Conformation of β-hairpins in protein structuresJournal of Molecular Biology, 1989
- Structural versatility of peptides from C?,?-dialkylated glycines. II. An IR absorption and1H-nmr study of homo-oligopeptides from C?,?-diethylglycineBiopolymers, 1988