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Conformational Preferences of Short Peptide Fragments
Author(s) -
Hatakeyama Yoshiyuki,
Sawada Tomohisa,
Kawano Masaki,
Fujita Makoto
Publication year - 2009
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.200903563
Subject(s) - peptide , folding (dsp implementation) , chemistry , crystallography , protein folding , protein structure , biophysics , biochemistry , biology , electrical engineering , engineering
Folding in the confine : Short fragments of tri‐ to hexapeptides have been encapsulated by a synthetic host in water and folded into their latent helical structures (see crystal structure). Crystallographic analysis of the complexes clearly reveals a mixed conformation of 3 10 and α helices, thereby illustrating the inherent helical propensity of very short peptide fragments.
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