1H NMR study of long and short myosin S2 fragments

FEBS Letters

Stewart, Murray²  Roberts, Gordon C.K.¹ 

[1] Division of Molecular Pharmacology, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, England;MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH England

关键词: Myosin;    Long S2;    Short S2;    NMR;    Hinge;    Fibrous protein;   

DOI  :  10.1016/0014-5793(82)80937-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The 270 MHz ¹H NMR spectra of rabbit skeletal long and short S2 were indistinguishable at 20°C and 30°C and contained only a small proportion of sharp peaks associated with flexible regions. At 60°C both proteins were denatured and had essentially identical spectra. At 40°C and 50°C the long S2 spectrum contained a marginally greater proportion of sharp peaks, representing not more than 25 residues/chain. Our results are consistent with the presence of a small hinge in long S2 but do not support its containing an extensive region which provides contractile force by a helix—coil transition.

【 授权许可】

Unknown