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.
Original language | English |
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Pages (from-to) | 647-654 |
Number of pages | 8 |
Journal | Biochemistry International |
Volume | 16 |
Issue number | 4 |
Publication status | Published - Apr 1988 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Biochemistry