Comparative Study
doi: 10.1111/j.1432-1033.1986.tb09978.x.
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
- PMID: 3769935
- DOI: 10.1111/j.1432-1033.1986.tb09978.x
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Comparative Study
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
Eur J Biochem.
.
Free article
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.
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