A high resolution 1H NMR study of the solution structure of human epidermal growth factor
- 1 September 1986
- journal article
- Published by Wiley in FEBS Letters
- Vol. 205 (1) , 77-81
- https://doi.org/10.1016/0014-5793(86)80869-9
Abstract
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.Keywords
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