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Natural polypeptide scaffolds: β‐sheets, β‐turns, and β‐hairpins
Author(s) -
Rotondi Kenneth S.,
Gierasch Lila M.
Publication year - 2005
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20390
Subject(s) - peptidomimetic , chemistry , side chain , stereochemistry , crystallography , biophysics , peptide , polymer , biochemistry , organic chemistry , biology
This paper provides an introduction to fundamental conformational states of polypeptides in the β‐region of φ,ψ space, in which the backbone is extended near to its maximal length, and to more complex architectures in which extended segments are linked by turns and loops. There are several variants on these conformations, and they comprise versatile scaffolds for presentation of side chains and backbone amides for molecular recognition and designed catalysts. In addition, the geometry of these fundamental folds can be readily mimicked in peptidomimetics. © 2005 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 84: 13–22, 2006 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com