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

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.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Miick SM,Todd AP,Millhauser GL

doi

10.1021/bi00103a016

subject

Has Abstract

pub_date

1991-10-01 00:00:00

pages

9498-503

issue

39

eissn

0006-2960

issn

1520-4995

journal_volume

30

pub_type

杂志文章

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