Open AccessA high‐resolution 1 H‐NMR study of human transforming growth factor α
Author(s) -
TAPPIN Michael J.,
COOKE Robert M.,
FITTON John E.,
CAMPBELL Iain D.
Publication year - 1989
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1989.tb14594.x
Subject(s) - histidine , epidermal growth factor , chemistry , nuclear overhauser effect , recombinant dna , nmr spectra database , tgf alpha , proton nmr , resolution (logic) , crystallography , titration , protein secondary structure , spectral line , protein tertiary structure , transforming growth factor , nuclear magnetic resonance spectroscopy , nuclear magnetic resonance , stereochemistry , physics , biology , amino acid , biochemistry , receptor , astronomy , artificial intelligence , computer science , gene , microbiology and biotechnology
The 500‐MHz and 600‐MHz 1 H‐NMR spectra of recombinant human transforming growth factor α have been recorded at pH values of 3.8, 6.5 and 9.4. Analysis of various two‐dimensional spectra has enabled sequence‐specific assignments to be made and the secondary structure to be identified. Information on the tertiary fold has also been obtained from observed nuclear Overhauser effects and titration of histidine residues. The overall fold of the protein is very similar to that of epidermal growth factor, as might be expected from the sequence similarity. However, the structure of transforming growth factor α at pH 3.8 is found to show interesting differences from those at the two higher pHs and from that of epidermal growth factor.