Premium
Study of global motions in proteins by weighted masses molecular dynamics: Adenylate kinase as a test case
Author(s) -
Elamrani Samir,
Berry Michael B.,
Phillips George N.,
McCammon J. Andrew
Publication year - 1996
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199605)25:1<79::aid-prot6>3.0.co;2-f
Subject(s) - adenylate kinase , molecular dynamics , flexibility (engineering) , set (abstract data type) , computer science , computational biology , biological system , molecular mass , dynamics (music) , chemistry , physics , biology , enzyme , biochemistry , mathematics , computational chemistry , statistics , programming language , acoustics
The weighted masses molecular dynamics (WMMD) technique is applied to the protein adenylate kinase. A novel set of restraints has been developed to allow the use of this technique with proteins. The WMMD simulation is successful in predicting the flexibility of the two mobile domains of the protein. The end product of the simulation is similar to the known open and AMP bound forms of the enzyme. The biological relevance of the restraints used and potential methods of improving the technique are discussed. © 1996 Wiley‐Liss, Inc.