Domain structure of myosin subfragment‐1

FEBS Letters

Shnyrov, Valery L.¹  Vedenkina, Natalia S.¹  Khvorov, Nikolai V.²  Permyakov, Eugene A.¹  Levitsky, Dmitrii I.²  Poglazov, Boris F.² 

[1] Institute of Biological Physics of the USSR Academy of Sciences, Pushchino, Moscow Region 142292, USSR;A.N. Bach Institute of Biochemistry of the USSR Academy of Sciences, Moscow 117071, USSR

关键词: Myosin subfragment-1;    Domain structure;    Scanning microcalorimetry;    Tryptophan fluorescence;    Rabbit skeletal muscle;   

DOI  :  10.1016/0014-5793(90)80242-B

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The structure of the myosin subfragment-1 (SI) from rabbit skeletal muscle was studied using differential scanning microcalorimetry. Three independently melting regions (domains) were revealed in S1. Selective denaturation of the middle 50 kDa segment of the S1 heavy chain resulted in the disappearance of the heat sorption peak corresponding to the melting of the first, the most thermolabile domain without any effect on the thermally induced blue shift of the intrinsic tryptophan fluorescence spectrum which occurs within the temperature region of melting of the second domain. It is concluded that the most thermolabile domain seems to correspond to the N-terminal part of the 50 kDa segment devoid of tryptophan residues.

【 授权许可】

Unknown