A comparison of the different helices adopted by α- and β-peptides suggests different reasons for their stability.
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ABSTRACT:
SUBMITTER: Allison JR
PROVIDER: S-EPMC3005789 | biostudies-literature | 2010 Nov
REPOSITORIES: biostudies-literature
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A comparison of the different helices adopted by α- and β-peptides suggests different reasons for their stability.
Allison Jane R JR Müller Marlen M van Gunsteren Wilfred F WF
Protein science : a publication of the Protein Society 20101101 11
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 particu ...[more]
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