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Can Helical Peptides Unwind One Turn at a Time? ‐ Controlled Conformational Transitions in α,β 2,3 ‐Hybrid Peptides
Author(s) -
Balamurugan Dhayalan,
Muraleedharan Kannoth M.
Publication year - 2015
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201501198
Subject(s) - polarity (international relations) , chemistry , turn (biochemistry) , conformational change , crystallography , biophysics , sequence (biology) , terminal (telecommunication) , stereochemistry , biochemistry , biology , computer science , cell , telecommunications
Unfolding of helical trans ‐β 2,3 ‐hybrid peptides with (α–β) n α composition, when executed by increasing solvent polarity or temperature, proceeded in a systematic manner with the turns unwinding sequentially; C‐terminal region of these peptides were first to unwind and the process propagated towards N terminus with more and more β residues equilibrating from the gauche to the anti rotameric state across C α C β . This is evidenced by clear change in their C β H signal splitting, 3 J CαH–CβH values, and sequential disappearance of i , i +2 NOEs.