A comparative 1H NMR study of mouse alpha(1-53) and beta(2-53) epidermal growth factors.
The three-dimensional structure of the mouse epidermal growth factor (EGF) in solution was studied by comparison of the 1H NMR spectra of alpha EGF (1-53) and beta EGF (2-53, des-asparaginyl 1 form). Using pH dependence of chemical shifts and a two-dimensional difference spectrum, the effect of the N-terminal deletion was investigated based on the complete assignment of the proton resonances. The affected residues were all found to be located exactly in the triple-stranded, beta-sheet core in the N-terminal domain of the EGF molecule.
Kohda
D
D
Department of Molecular Physiology, Tokyo Metropolitan Institute of Medical Science, Japan.
Kodama
C
C
Kase
R
R
Nomoto
H
H
Hayashi
K
K
Inagaki
F
F
D000596:Amino Acids; D000818:Animals; D004815:Epidermal Growth Factor / Q000302:isolation & purification; D009682:Magnetic Resonance Spectroscopy; D008297:Male; D051379:Mice; D011487:Protein Conformation; D013363:Submandibular Gland / Q000032:analysis
D000596:Amino Acids; D004815:Epidermal Growth Factor