The interplay between protein dynamics and frustration of non-bonded interactions as revealed by molecular dynamics simulations
- Author
- TAVERNELLI, Ivano1 ; DI IORIO, Ernesto E1
[1] Institute of Biochemistry, Swiss Federal Institute of Technology (ETH)-Zentrum, Universitätstrasse 16, 8092 Zurich, Switzerland - Source
Chemical physics letters. 2001, Vol 345, Num 3-4, pp 287-294 ; ref : 17 ref
- CODEN
- CHPLBC
- ISSN
- 0009-2614
- Scientific domain
- General chemistry, physical chemistry; Atomic molecular physics; Condensed state physics
- Publisher
- Elsevier Science, Amsterdam
- Publication country
- Netherlands
- Document type
- Article
- Language
- English
- Keyword (fr)
- Changement conformation Energie interaction Fonction corrélation temps Interaction moléculaire Interaction électrostatique Molécule flexible Méthode dynamique moléculaire Pliage Protéine Rubrédoxine Simulation numérique
- Keyword (en)
- Conformational changes Interaction energy Time correlation function Molecular interaction Electrostatic interaction Flexible molecule Molecular dynamics method Folding Protein Rubredoxin Numerical simulation
- Keyword (es)
- Energía interacción Función correlación tiempo Interacción molecular Interacción electrostática Molécula flexible Método dinámico molecular Doblado Proteína Rubredoxina Simulación numérica
- Classification
- Pascal
- 002 Biological and medical sciences / 002A Fundamental and applied biological sciences. Psychology / 002A03 Molecular biophysics / 002A03I Conformational dynamics in molecular biology
- Discipline
- Molecular biophysics
- Origin
- Inist-CNRS
- Database
- PASCAL
- INIST identifier
- 14102148
Sauf mention contraire ci-dessus, le contenu de cette notice bibliographique peut être utilisé dans le cadre d’une licence CC BY 4.0 Inist-CNRS / Unless otherwise stated above, the content of this bibliographic record may be used under a CC BY 4.0 licence by Inist-CNRS / A menos que se haya señalado antes, el contenido de este registro bibliográfico puede ser utilizado al amparo de una licencia CC BY 4.0 Inist-CNRS
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DOI
10.1016/S0009-2614(01)00859-4 
https://dx.doi.org/10.1016/S0009-2614(01)00859-4
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