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1H-NMR study of mobility and conformational constraints within the proline-rich N-terminal of the LC1 alkali light chain of skeletal myosin. Correlation with similar segments in other protein systems.

作者信息

Bhandari D G, Levine B A, Trayer I P, Yeadon M E

出版信息

Eur J Biochem. 1986 Oct 15;160(2):349-56. doi: 10.1111/j.1432-1033.1986.tb09978.x.

DOI:10.1111/j.1432-1033.1986.tb09978.x
PMID:3769935
Abstract

Analysis by 1H-NMR spectroscopic techniques of the conformation of the N-terminal segment of the LC1 alkali light chain of rabbit skeletal muscle has shown that this portion of the molecule adopts a well-defined elongated configuration. This rod-like feature is a consequence of the Ala/Pro-rich composition and the functional aspects of such conformational preference in this and similar segments in other proteins are discussed.

摘要

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