Solvent-induced forces (SIFs) acting on single residues of BPTI (bovine pancreatic trypsin inhibitor) are obtained by molecular dynamics simulations. Our procedure takes into full account the demonstrated inherently strong non-additivity of SIFs. Cross-correlations of instantaneous SIFs on distant residue pairs endorse the view that SIFs are caused by the concurrent action of all residues on solvent configurations. This agrees with the many-body character of the potential of mean force. The elicited collective origin of SIFs helps towards a sounder understanding of their role.
Correlated solvent-induced forces on a protein at single residue resolution: relation to conformation, stability, dynamics and function
V Martorana;
1996
Abstract
Solvent-induced forces (SIFs) acting on single residues of BPTI (bovine pancreatic trypsin inhibitor) are obtained by molecular dynamics simulations. Our procedure takes into full account the demonstrated inherently strong non-additivity of SIFs. Cross-correlations of instantaneous SIFs on distant residue pairs endorse the view that SIFs are caused by the concurrent action of all residues on solvent configurations. This agrees with the many-body character of the potential of mean force. The elicited collective origin of SIFs helps towards a sounder understanding of their role.File in questo prodotto:
Non ci sono file associati a questo prodotto.
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
