Proton NMR studies of denatured lysozyme

FEBS Letters

Dobson, Christopher M.¹  Evans, Philip A.¹  Williamson, Kenneth L.¹ 

[1] Inorganic Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QR, England

关键词: 1H NMR;    Lysozyme;    Protein denaturation;    Protein folding;    Saturation transfer;    DMSO;    dimethyl sulfoxide;   

DOI  :  10.1016/0014-5793(84)80273-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Evidence is presented from ¹H NMR studies for non-random conformational behaviour in denatured lysozyme in aqueous solution. A method is presented which permits the assignment of resonances in the ¹H NMR spectrum of the denatured protein by observing magnetisation transfer from resonances of the native state. The use of these experiments in characterising the denatured state and the significance of these studies for the investigation of protein folding are discussed.

【 授权许可】

Unknown