Mobility-based prediction of hydration structures of protein surfaces.
Bioinformatics
; 31(12): 1959-65, 2015 Jun 15.
Article
em En
| MEDLINE
| ID: mdl-25682067
ABSTRACT
MOTIVATION Hydration largely determines solubility, aggregation of proteins and influences interactions between proteins and drug molecules. Despite the importance of hydration, structural determination of hydration structure of protein surfaces is still challenging from both experimental and theoretical viewpoints. The precision of experimental measurements is often affected by fluctuations and mobility of water molecules resulting in uncertain assignment of water positions. RESULTS:
Our method can utilize mobility as an information source for the prediction of hydration structure. The necessary information can be produced by molecular dynamics simulations accounting for all atomic interactions including water-water contacts. The predictions were validated and tested by comparison to more than 1500 crystallographic water positions in 20 hydrated protein molecules including enzymes of biomedical importance such as cyclin-dependent kinase 2. The agreement with experimental water positions was larger than 80% on average. The predictions can be particularly useful in situations where no or limited experimental knowledge is available on hydration structures of molecular surfaces. AVAILABILITY AND IMPLEMENTATION The method is implemented in a standalone C program MobyWat released under the GNU General Public License, freely accessible with full documentation at http//www.mobywat.com.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Conformação Proteica
/
Algoritmos
/
Água
/
Quinase 2 Dependente de Ciclina
/
Simulação de Dinâmica Molecular
Tipo de estudo:
Prognostic_studies
/
Risk_factors_studies
Limite:
Humans
Idioma:
En
Revista:
Bioinformatics
Assunto da revista:
INFORMATICA MEDICA
Ano de publicação:
2015
Tipo de documento:
Article