Short alanine-based peptides may form 3(10)-helices and not alpha-helices in aqueous solution.

Abstract:

:Short alanine peptides, containing 16 or 17 residues, appear to form alpha-helices in aqueous solution. But the main spectroscopic analyses used on helical peptides (circular dichroism and nuclear magnetic resonance) cannot distinguish between an alpha-helix (in which the ith residue is hydrogen-bonded to residue i + 4; ref. 9) and the next most common peptide helix, the 3(10)-helix10 (i-->i + 3 hydrogen-bonding). To address this problem we have designed 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. Here we report the circular dichroism, Fourier-transform infrared and electron-spin resonance spectra of these peptides under helix-forming conditions. The infrared absorbance gives an amide I' band with a frequency that is substantially different from that observed for alpha-helices. The electron-spin resonance spectra of doubly labelled helices show that the ranking of distances between side chains, around a single turn (residues 4-8), is inconsistent with an alpha-helical structure. Our experiments suggest that the more likely peptide geometry is a 3(10)-helix.

journal_name

Nature

journal_title

Nature

authors

Miick SM,Martinez GV,Fiori WR,Todd AP,Millhauser GL

doi

10.1038/359653a0

keywords:

subject

Has Abstract

pub_date

1992-10-15 00:00:00

pages

653-5

issue

6396

eissn

0028-0836

issn

1476-4687

journal_volume

359

pub_type

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