Abstract
Three 1 ns-long molecular dynamics (MD) simulations were performed on murine epidermal growth factor (mEGF), human epidermal growth factor (hEGF) and human transforming growth factor-alpha (hTGF-α) to obtain further information about their conformational properties. The initial structures were taken based on NMR spectroscopy data and were energy-minimized before MD simulations. No major conformational transitions were observed during simulations. Domain movements, predictable from the mitten model of EGF, were observed only in the simulation of hTGF-α and could account for its different receptor binding properties. Inter-domain interactions, not revealed by the NMR data, were observed between aromatic side-chains for each of the polypeptides and seem to stabilize the conformation necessary for binding.
Original language | English (US) |
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Pages (from-to) | 543-550 |
Number of pages | 8 |
Journal | Journal of Molecular Structure: THEOCHEM |
Volume | 398-399 |
DOIs | |
State | Published - Jun 30 1997 |
All Science Journal Classification (ASJC) codes
- Biochemistry
- Condensed Matter Physics
- Physical and Theoretical Chemistry