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Position-dependent local motions in spin-labeled analogues of a short alpha-helical peptide determined by electron spin resonance.

Authors
Type
Published Article
Journal
Biochemistry
Publisher
American Chemical Society
Volume
30
Issue
39
Pages
9498–9503
Source
UCSC Aging biomedical-ucsc
License
Unknown

Abstract

We have used electron spin resonance and circular dichroism to examine and compare the dynamics in two analogues of the Ala-based 3K(I) peptide [Marqusee, S., Robbins, V.H., & Baldwin, R. L. (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 5286-5290], labeled at positions 4 and 8, throughout the alpha-helix——coil transition. In the middle of the thermal unfolding transition, our results demonstrate that the local mobility near the N-terminus is greater than at the center of the peptide. This provides evidence, from the perspective of dynamics, that the ends of Ala-based alpha-helices are frayed. We further find that the position dependence of the mobility for the thermally unfolded state differs from that of the denaturant unfolded state. Only the latter state exhibits the local dynamics expected for a genuine random coil.

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