Unexpectedly strong energy stabilization inside the hydrophobic core of small protein rubredoxin mediated by aromatic residues: correlated ab initio quantum chemical calculations
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
15725017
DOI
10.1021/ja044607h
Knihovny.cz E-resources
- MeSH
- Hydrophobic and Hydrophilic Interactions MeSH
- Protein Conformation MeSH
- Quantum Theory MeSH
- Models, Molecular MeSH
- Rubredoxins chemistry MeSH
- Protein Folding MeSH
- Thermodynamics MeSH
- Structure-Activity Relationship MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Rubredoxins MeSH
The formation of a hydrophobic core of globular proteins is believed to be the consequence of exterior hydrophobic forces of entropic nature. This, together with the low occurrence of hydrogen bonds in the protein core, leads to the opinion that the energy contribution of core formation to protein folding and stability is negligible. We show that stabilization inside the hydrophobic core of a small protein, rubredoxin, determined by means of high-level correlated ab initio calculations (complete basis set limit of MP2 stabilization energy + CCSD(T) correction term), amounted to approximately 50 kcal/mol. These results clearly demonstrate strong attraction inside a hydrophobic core. This finding may lead to substantial changes in the current view of protein folding. We also point out the inability of the DFT/B3LYP method to describe a strong attraction between studied amino acids.
J Am Chem Soc. 2005 Jun 8;127(22):8232 PubMed
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