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A Conformational Flexibility Scale for Amino Acids in Peptides
Author(s) -
Huang Fang,
Nau Werner M.
Publication year - 2003
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/anie.200250684
Subject(s) - flexibility (engineering) , amino acid , scale (ratio) , chemistry , computer science , computational biology , biochemistry , biology , mathematics , geography , cartography , statistics
The end‐to‐end collision frequency of short polypeptides labeled with a fluorescent probe (DBO) at one end and an efficient contact quencher (Trp) at the other end (see scheme) provides an absolute measure of the time scale of conformational changes in short structureless peptides as a function of the amino acid type. A general correlation with secondary structure propensity applies, with the most flexible amino acids being most abundant in β turns and the most rigid ones in β sheets.