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Langevin dynamics of proteins at constant pH.

Langevin dynamics of proteins at constant pH.

Authors :
Walczak AM
Antosiewicz JM
Source :
Physical review. E, Statistical, nonlinear, and soft matter physics [Phys Rev E Stat Nonlin Soft Matter Phys] 2002 Nov; Vol. 66 (5 Pt 1), pp. 051911. Date of Electronic Publication: 2002 Nov 20.
Publication Year :
2002

Abstract

An application of the Langevin dynamics algorithm for simulation of protein conformational equilibria at constant pH is presented. The algorithm is used to compute average protonation of titratable groups in ovomucoid third domain, as functions of pH, resulting in data, basically equivalent to the pH dependencies of chemical shifts obtained from multidimensional nuclear magnetic resonance (NMR) spectroscopy, for the protein titratable residues. The pK(a) values obtained from the simulation are in reasonable agreement with experimental data. Possible improvements of this methodology, using achievements from other fields of mesoscopic biomolecular simulations, are also discussed.

Details

Language :
English
ISSN :
1539-3755
Volume :
66
Issue :
5 Pt 1
Database :
MEDLINE
Journal :
Physical review. E, Statistical, nonlinear, and soft matter physics
Publication Type :
Academic Journal
Accession number :
12513527
Full Text :
https://doi.org/10.1103/PhysRevE.66.051911