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 |
|---|---|
| Pages (from-to) | 543-550 |
| Number of pages | 8 |
| Journal | Journal of Molecular Structure: THEOCHEM |
| Volume | 398-399 |
| State | Published - Jun 30 1997 |
Fingerprint
All Science Journal Classification (ASJC) codes
- Physical and Theoretical Chemistry
- Computational Theory and Mathematics
- Atomic and Molecular Physics, and Optics
Cite this
Molecular dynamics simulation of egf and tgf-α : Conformation and receptor binding properties. / Lovas, Sándor; Murphy, Richard F.
In: Journal of Molecular Structure: THEOCHEM, Vol. 398-399, 30.06.1997, p. 543-550.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Molecular dynamics simulation of egf and tgf-α
T2 - Conformation and receptor binding properties
AU - Lovas, Sándor
AU - Murphy, Richard F.
PY - 1997/6/30
Y1 - 1997/6/30
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0001603162&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0001603162&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:0001603162
VL - 398-399
SP - 543
EP - 550
JO - Computational and Theoretical Chemistry
JF - Computational and Theoretical Chemistry
SN - 2210-271X
ER -