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A Comparison of the Different Helices Adopted by α‐ and β‐Peptides Suggests Different Reasons for Their Stability by Jane R. Allison; Marlen Müller; Wilfred F. van Gunsteren is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract 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.

Who reads A Comparison of the Different Helices Adopted by α‐ and β‐Peptides Suggests Different Reasons for Their Stability?

Author

Jane R. Allison; Marlen Müller; Wilfred F. van Gunsteren

Publisher

Cold Spring Harbor Laboratory Press; Wiley (John Wiley & Sons); Wiley-Blackwell; Wiley (ISSN 0961-8368)

Published

2010

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)