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Spin Relaxation Enhancement Confirms Dominance of Extended Conformations in Short Alanine Peptides
Author(s) -
Chen Kang,
Liu Zhigang,
Zhou Chunhui,
Bracken W. Clay,
Kallenbach Neville R.
Publication year - 2007
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.200703376
Subject(s) - random coil , alanine , relaxation (psychology) , population , chemistry , nuclear magnetic resonance , peptide , crystallography , chemical physics , physics , materials science , amino acid , biology , biochemistry , neuroscience , circular dichroism , demography , sociology
Local order goes with random coil : An ensemble of peptide structures is generated with over 90 % extended conformation for Ala and Pro. The population‐averaged long‐range distance from the N‐terminal spin‐label residue (see picture, red dot) to the C‐terminal amide proton of Ala (blue dots) is fully consistent with the results from NMR spin relaxation measurements.