<sup>1</sup>H-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.

BHANDARI D G; LEVINE B A; TRAYER I P; YEADON M E

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J-GLOBAL ID：200902047539031552 Reference number：87A0086677

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.

骨格筋ミオシンのLC1アルカリ軽鎖のプロリンに富むN-末端内の移動度と立体配座拘束についての¹H-NMRによる研究他の蛋白質系での似た断片との相関

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Volume： 160 Issue： 2 Page： 349-356 Publication year： Oct. 15, 1986
JST Material Number： B0206B ISSN： 0014-2956 CODEN： EJBCAI Document type： Article
Article type：原著論文 Country of issue： United Kingdom (GBR) Language： ENGLISH (EN)

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Proteins and peptides in general , Muscles

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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.

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.