[sup1]H-NMR study of mobility and conformational constraints within the proline-rich N-terminal of the LC1 alkali light chain of skeletal myosin.

Reports on an analysis of [sup 1]hydrogen-nuclear magnetic resonance spectroscopic techniques of the conformation of the nitrogen terminal segment of the LC1 alkali light chain of rabbit skeletal muscle which has shown that this portion of the molecule adopts a well-defined elongated configuration. Finding that the rod-like feature is a consequence of the Ala/Pro-rich composition and discussion of the functional aspects of such conformational preference in this and similar segments in other proteins.