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Short alanine-based peptides may form 3(10)-helices and not alpha-helices in aqueous solution.
The experiments suggest that the more likely peptide geometry is a 3(10)-helix, and single and doubly spin-labelled analogues of alanine-based peptides in which the nitroxide spin label forms an unbranched side chain extending from the sulphur atom of a cysteine residue are designed.
Exploring the peptide 3(10)-helix reversible alpha-helix equilibrium with double label electron spin resonance.
There is a significant amount of 3(10)-helix in 16-residue model peptides containing only L-amino acids and the role of Arg+ in the stabilization of specific helix structures is found.
Increasing sequence length favors alpha-helix over 3(10)-helix in alanine-based peptides: evidence for a length-dependent structural transition.
The data indicate that the proportion of alpha-helix and 3(10)-helix in Ala-based peptides depends upon the sequence length.
The nucleation of monomeric parallel beta-sheet-like structures and their self-assembly in aqueous solution.
A single carboxy-terminal arginine determines the amino-terminal helix conformation of an alanine-based peptide
Findings suggest that a single strategically-placed arginine can exert long range control on helix structure, by examining how Lys+→Arg+ substitutions influence the 310-helix→α-helIX equilibrium in the helical peptide Ac-(AAAAK)3A-NH2.
Short alanine-based peptides may form 310-helices and not α-helices in aqueous solution
The experiments suggest that the more likely peptide geometry is a 310-helix, and single and doubly spin-labelled analogues of alanine-based peptides in which the nitroxide spin label forms an unbranched side chain extending from the sulphur atom of a cysteine residue are designed.
Alanine is helix-stabilizing in both template-nucleated and standard peptide helices.
- C. Rohl, W. Fiori, R. L. Baldwin
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 30 March 1999
A model in which the helix propensities of residues at the template-peptide junction are treated separately brings the results from alanine-based peptides and template-nucleated helices into agreement and provides a physically plausible resolution of the discrepancies between the two systems.
Exploring the peptide 310‐helix ⇆ α–helix equilibrium with double label electron spin resonance
A review of spin labeling strategy, interpretation of ESR spectra and the influence of molecular dynamics on the spectral line shapes finds that there is a significant amount of 310–helix in 16–residue model peptides containing only L–amino acids.