title: The third leg: molecular dynamics simulations of lipid binding proteins.
abstract: Molecular dynamics computer simulations can provide a third leg which balances the contributions of both structural biology and binding studies performed on the lipid binding protein family. In this context, these calculations help to establish a dialogue between all three communities, by relating experimental observables with details of structure. Working towards this connection is important, since experience has shown the difficulty of inferring thermodynamic properties from a single static conformation. The challenge is exemplified by ongoing attempts to interpret the impact of mutagenesis on structure and function (i.e. binding). A detailed atomic-level understanding of this system could be achieved with the support of all three legs, paving the way towards rational design of proteins with novel specificities. This paper provides an outline of the connections possible between experiment and theory concerning lipid binding proteins.
authors.affiliation: Johns Hopkins University, Department of Physiology, Baltimore, MD 21205, USA.
authors.forename: T B
authors.initials: TB
authors.lastname: Woolf
authors.forename: M
authors.initials: M
authors.lastname: Tychko
mesh_terms: D002352:Carrier Proteins / Q000737:chemistry*; D003198:Computer Simulation; D050556:Fatty Acid-Binding Proteins; D007700:Kinetics; D008958:Models, Molecular; D009154:Mutation; D018996:Myelin P2 Protein / Q000737:chemistry*; D009363:Neoplasm Proteins; D019301:Oleic Acid / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D012984:Software; D013997:Time Factors; D014867:Water / Q000737:chemistry
chemical_list: D002352:Carrier Proteins; D050556:Fatty Acid-Binding Proteins; D018996:Myelin P2 Protein; D009363:Neoplasm Proteins; D014867:Water; D019301:Oleic Acid