| Literature DB >> 3260496 |
D Kohda1, C Kodama, R Kase, H Nomoto, K Hayashi, F Inagaki.
Abstract
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.Entities:
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Year: 1988 PMID: 3260496
Source DB: PubMed Journal: Biochem Int ISSN: 0158-5231