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A Designed β ‐Hairpin Containing a Natural Hydrophobic Cluster
Author(s) -
Espinosa Juan F.,
Gellman Samuel H.
Publication year - 2000
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20000703)39:13<2330::aid-anie2330>3.0.co;2-c
Subject(s) - antiparallel (mathematics) , chemistry , hydrophobic effect , aqueous solution , cluster (spacecraft) , residue (chemistry) , proline , crystallography , stereochemistry , side chain , amino acid , biophysics , biochemistry , organic chemistry , physics , biology , computer science , polymer , quantum mechanics , magnetic field , programming language
Designer hairpins: 12‐Residue peptide 1 , containing D ‐proline, folds to form a two‐stranded antiparallel β ‐sheet in aqueous solution, which causes clustering of the side chains of Trp 2, Tyr 4, Phe 11, and Val 13 (highlighted in the drawing). A similar cluster occurs in the folded state of the protein GB1. Thermodynamic analysis suggests that both the hydrophobic effect and intrinsic interstrand attractions contribute to β ‐hairpin stability.