A mesoscopic model for protein-protein interactions in solution.

ABSTRACT: Protein self-association may be detrimental in biological systems, but can be utilized in a controlled fashion for protein crystallization. It is hence of considerable interest to understand how factors like solution conditions prevent or promote aggregation. Here we present a computational model describing interactions between protein molecules in solution. The calculations are based on a molecular description capturing the detailed structure of the protein molecule using x-ray or nuclear magnetic resonance structural data. Both electrostatic and van der Waals interactions are included and the salt particles are explicitly treated allowing investigations of systems containing mono-, di-, and trivalent ions. For three different proteins-lysozyme, alpha-chymotrypsinogen, and calbindin D(9k)

SUBMITTER: Lund M 

PROVIDER: S-EPMC1303572 | biostudies-literature | 2003 Nov

REPOSITORIES: biostudies-literature