A high resolution 1H NMR study of the solution structure of human epidermal growth factor

FEBS Letters

Gregory, H.¹  Carver, J.A.¹  Esposito, G.¹  Sheard, B.¹  Campbell, I.D.¹  Cooke, R.M.¹ 

[1] Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU England

关键词: Growth factor;    (Human EGF);    NMR;    Protein structure;   

DOI  :  10.1016/0014-5793(86)80869-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

500 MHz ¹H NMR studies of human epidermal growth factor are described. The backbone resonances of the 1–48 derivative of hEGF have been assigned using two-dimensional techniques. Analysis of the type and magnitude of the observed sequential nuclear Overhauser effects and the NH-αCH spin-spin coupling constants allowed prediction of the secondary structure. Aspects of the tertiary structure are also identified. A pair of antiparallel β-sheets involving residues 18–23 and 28–34 is a dominant feature of the solution structure.

【 授权许可】

Unknown