Computational studies on mutant protein stability: The correlation between surface thermal expansion and protein stability
| Autor: | Paul M. G. Curmi, Rocio Palma |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Protein Conformation
Mutant Plasma protein binding Biochemistry Accessible surface area Molecular dynamics Protein structure Ribonucleases Bacterial Proteins Mutant protein Bacteriophage T4 Thermal stability Computer Simulation Molecular Biology Barnase biology Chemistry Temperature Crystallography Kinetics Models Chemical Mutagenesis Biophysics biology.protein Thermodynamics Muramidase Protein Binding Research Article |
| Zdroj: | Protein science : a publication of the Protein Society. 8(4) |
| ISSN: | 0961-8368 |
| Popis: | Thermal stability of mutant proteins has been investigated using temperature dependent molecular dynamics (MD) simulations in vacuo. The numerical modeling was aimed at mimicking protein expansion upon heating. After the conditions for an expanding protein accessible surface area were established for T4 lysozyme and barnase wild-type proteins, MD simulations were carried out under the same conditions using the crystal structures of several mutant proteins. The computed thermal expansion of the accessible surface area of mutant proteins was found to be strongly correlated with their experimentally measured stabilities. A similar, albeit weaker, correlation was observed for model mutant proteins. This opens the possibility of obtaining stability information directly from protein structure. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text