A high-resolution 1H-NMR study of human transforming growth factor alpha. Structure and pH-dependent conformational interconversion.
The 500-MHz and 600-MHz 1H-NMR spectra of recombinant human transforming growth factor alpha 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 alpha at pH 3.8 is found to show interesting differences from those at the two higher pHs and from that of epidermal growth factor.
Tappin
M J
MJ
Department of Biochemistry, University of Oxford, England.
Cooke
R M
RM
Fitton
J E
JE
Campbell
I D
ID
D004815:Epidermal Growth Factor; D004926:Escherichia coli; D006801:Humans; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000096:biosynthesis; D013696:Temperature; D015291:Transforming Growth Factors / Q000096:biosynthesis
D011994:Recombinant Proteins; D004815:Epidermal Growth Factor; D015291:Transforming Growth Factors