Nuclear-magnetic-resonance studies of human epidermal growth factor.
The 1H-NMR spectra of native human epidermal growth factor (EGF) and a derivative lacking the final five residues have been assigned by two-dimensional methods, enabling their structures to be compared. The same structural features are observed for each protein, although the final five residues of native human EGF interact with residues earlier in the sequence. Comparison of the resonance shifts of human, rat and mouse EGF and human transforming growth factor alpha (TGF alpha) enables shifts characteristic of the EGF conformation to be identified, providing standards by which the structures of related proteins may be assessed.
Cooke
R M
RM
Department of Biochemistry, University of Oxford, UK.
Tappin
M J
MJ
Campbell
I D
ID
Kohda
D
D
Miyake
T
T
Fuwa
T
T
Miyazawa
T
T
Inagaki
F
F
D000595:Amino Acid Sequence; D000818:Animals; D004815:Epidermal Growth Factor / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D051379:Mice; D008969:Molecular Sequence Data; D011487:Protein Conformation; D051381:Rats; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D012689:Sequence Homology, Nucleic Acid
D011993:Recombinant Fusion Proteins; D004815:Epidermal Growth Factor; D006859:Hydrogen