A Conformational Flexibility Scale for Amino Acids in Peptides

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 t...

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Bibliographic Details
Published inAngewandte Chemie (International ed.) Vol. 42; no. 20; pp. 2269 - 2272
Main Authors Huang, Fang, Nau, Werner M.
Format Journal Article
LanguageEnglish
Published Weinheim WILEY-VCH Verlag 25.05.2003
WILEY‐VCH Verlag
Subjects
amino acids
Amino Acids - chemistry
Amino Acids - metabolism
Deuterium - metabolism
fluorescence
Molecular Structure
peptides
Peptides - chemistry
Peptides - metabolism
Protein Conformation
protein folding
secondary structure
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Summary: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.
Bibliography:ArticleID:ANIE200250684
ark:/67375/WNG-7RD9PVPW-F
This work was supported by the Swiss National Science Foundation within the NFP 47 "Supramolecular Functional Materials".
istex:6FB91E71B3D3618098B975158B5E1829B080433D
This work was supported by the Swiss National Science Foundation within the NFP 47 “Supramolecular Functional Materials”.
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SourceType-Scholarly Journals-1
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ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200250684