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Structural features and conformational equilibria of 3 10 ‐helical peptides in solution by spectroscopic and molecular mechanics studies
Author(s) -
Pispisa B.,
Mazzuca C.,
Palleschi A.,
Stella L.,
Venanzi M.,
Formaggio F.,
Toniolo C.,
Broxterman Q. B.
Publication year - 2002
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.10118
Subject(s) - chemistry , molecular mechanics , förster resonance energy transfer , protein secondary structure , helix (gastropod) , molecular dynamics , molecular conformation , molecular orbital , crystallography , fluorescence , computational chemistry , molecule , organic chemistry , biochemistry , ecology , physics , quantum mechanics , snail , biology
The structural features and conformational equilibria of a series of short, linear C α ‐methylvaline [(αMe)Val]‐based peptides in methanol were investigated by combining fluorescence resonance energy transfer measurements and molecular mechanics data. IR spectra were employed to determine their secondary structure, which exhibits an intramolecularly H‐bonded, 3 10 ‐helix conformation that is affected by backbone distortions that are enhanced by the shortness of the main chain. © 2002 Wiley Periodicals, Inc. Biopolymers (Biospectroscopy) 67: 247–250, 2000