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.
D000199:Actins / Q000378:metabolism; D000409:Alanine / Q000032:analysis; D001665:Binding Sites; D009682:Magnetic Resonance Spectroscopy; D015879:Myosin Subfragments; D009218:Myosins / Q000302:isolation & purification*; D010446:Peptide Fragments / Q000302:isolation & purification*; D011392:Proline / Q000032:analysis*; D011487:Protein Conformation
D000199:Actins; D015879:Myosin Subfragments; D010446:Peptide Fragments; D011392:Proline; D009218:Myosins; D000409:Alanine