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A comparison of the different helices adopted by α‐ and β‐peptides suggests different reasons for their stability
Author(s) -
Allison Jane R.,
Müller Marlen,
van Gunsteren Wilfred F.
Publication year - 2010
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.504
Subject(s) - protonation , helix (gastropod) , dipole , chemistry , molecular dynamics , solvent , solvent polarity , polarity (international relations) , peptide , crystallography , accessible surface area , computational chemistry , stereochemistry , biochemistry , organic chemistry , biology , ion , ecology , snail , cell
The right‐handed α‐helix is the dominant helical fold of α‐peptides, whereas the left‐handed 3 14 ‐helix is the dominant helical fold of β‐peptides. Using molecular dynamics simulations, the properties of α‐helical α‐peptides and 3 14 ‐helical β‐peptides with different C‐terminal protonation states and in the solvents water and methanol are compared. The observed energetic and entropic differences can be traced to differences in the polarity of the solvent‐accessible surface area and, in particular, the solute dipole moments, suggesting different reasons for their stability.