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A high resolution 1 H NMR study of the solution structure of human epidermal growth factor
Author(s) -
Carver J.A.,
Cooke R.M.,
Esposito G.,
Campbell I.D.,
Gregory H.,
Sheard B.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80869-9
Subject(s) - antiparallel (mathematics) , chemistry , nuclear overhauser effect , crystallography , nuclear magnetic resonance spectroscopy , resolution (logic) , protein secondary structure , stereochemistry , nuclear magnetic resonance , protein tertiary structure , physics , biochemistry , quantum mechanics , artificial intelligence , magnetic field , computer science
500 MHz 1 H 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.