Abstract.
Geometric properties of the RGD sequence in a data set of protein crystal and NMR structures deposited in the Protein Data Bank were examined to identify structural characteristics that are related to cell adhesion activity. Interatomic distances and dihedral angles are examined. These geometric measures are then used in an analysis of the conformations of the RGDW and DRGDW peptides obtained from molecular dynamics simulations (Stote RH, et al. (2000) J Phys ChemB 104:1624). This analysis leads to the suggestion that differences in the accessible conformations contribute to the difference in biological activity between the RGDW and the DRGDW peptides.
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Received: 15 August 2000 / Accepted: 4 October 2000 / Published online: 21 March 2001
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Stote, R. Analysis of the RGD sequence in protein structures: comparison to the conformations of the RGDW and DRGDW peptides determined by molecular dynamics simulations. Theor Chem Acc 106, 128–136 (2001). https://doi.org/10.1007/s002140000213
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DOI: https://doi.org/10.1007/s002140000213