The applicants plan to further develop computer algorithms to study the effects of environmental factors on oligopeptide peptide folding. In particular they are interested in the effects of pH on the folding of peptides with ionizable protons. This is viewed as a multi-step process where: 1) the pH changes the ionization state, 2) this in turn polarizes the solvent in the micro-environment, and 3) this in turn has direct effects on the peptide folding pattern.
| Vila, Jorge A; Ripoll, Daniel R; Baldoni, Hector A et al. (2002) Unblocked statistical-coil tetrapeptides and pentapeptides in aqueous solution: a theoretical study. J Biomol NMR 24:245-62 |
| Vila, J A; Ripoll, D R; Scheraga, H A (2001) Influence of lysine content and pH on the stability of alanine-based copolypeptides. Biopolymers 58:235-46 |
| Vila, J A; Ripoll, D R; Scheraga, H A (2000) Physical reasons for the unusual alpha-helix stabilization afforded by charged or neutral polar residues in alanine-rich peptides. Proc Natl Acad Sci U S A 97:13075-9 |
| Ripoll, D R; Vila, J A; Villegas, M E et al. (1999) On the pH-conformational dependence of the unblocked SYPYD peptide. J Mol Biol 292:431-40 |
| Vila, J A; Ripoll, D R; Villegas, M E et al. (1998) Role of hydrophobicity and solvent-mediated charge-charge interactions in stabilizing alpha-helices. Biophys J 75:2637-46 |
