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.

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.