Mass-weighted molecular dynamics simulation of the protein-ligand complex of rhizopuspepsin and inhibitor

• Published in: Biophysical journal Vol. 60; no. 4; pp. 966 - 973
• Main Author: Mao, B.
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Elsevier Inc 01.10.1991; Biophysical Society
• Subjects: Amino Acid Sequence; Aspartic Acid Endopeptidases - antagonists & inhibitors; Aspartic Acid Endopeptidases - metabolism; aspartic proteinases; binding sites; Biological and medical sciences; computer simulation; Conformational dynamics in molecular biology; crystals; Fundamental and applied biological sciences. Psychology; Ligands; Models, Molecular; Molecular biophysics; molecular conformation; Molecular Sequence Data; Molecular Weight; Oligopeptides - metabolism; Protease Inhibitors - metabolism; Protein Binding; Protein Conformation; proteinase inhibitors; Rhizopus; rhizopus chinensis; simulation models; Ligand binding; Enzyme; Conformational dynamics; Enzyme inhibitor; Inhibitor enzyme complex; Pepsin; Binding site; Spatial structure; Conformation

The mass-weighted molecular dynamics simulation method was developed previously for sampling the multidimensional conformational space of linear and cyclic polypeptides and studying their conformational flexibility. Herein results from molecular dynamics simulations of the protein-ligand complex of...