title: Conformational changes in protein function.
abstract: Conformational changes are the hallmarks of protein dynamics and are often intimately related to protein functions. Molecular dynamics (MD) simulation is a powerful tool to study the time-resolved properties of protein structure in atomic details. In this chapter, we discuss the various applications of MD simulation to the study of protein conformational changes, and introduce several selected advanced techniques that may significantly increase the sampling efficiencies, including locally enhanced sampling (LES), and grow-to-fit molecular dynamics (G2FMD).
authors.affiliation: Genome Center, University of California, Davis, CA, USA.
authors.forename: Haiguang
authors.initials: H
authors.lastname: Liu
authors.forename: Shubhra Ghosh
authors.initials: SG
authors.lastname: Dastidar
authors.forename: Hongxing
authors.initials: H
authors.lastname: Lei
authors.forename: Wei
authors.initials: W
authors.lastname: Zhang
authors.forename: Matthew C
authors.initials: MC
authors.lastname: Lee
authors.forename: Yong
authors.initials: Y
authors.lastname: Duan
mesh_terms: D003198:Computer Simulation; D007700:Kinetics; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry
chemical_list: D010455:Peptides; D011506:Proteins