Unexpectedly Strong Energy Stabilization Inside the Hydrophobic Core of Small Protein Rubredoxin Mediated by Aromatic Residues: Correlated Ab Initio Quantum Chemical Calculations

2005/02/05 by Jiřı́ Vondrášek, Lada Bendová, Vojtěch Klusák +1 · 2 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · #Hemoglobin structure and function #Protein Structure and Dynamics #Porphyrin Metabolism and Disorders #Rubredoxin #Chemistry #Ab initio #Quantum chemical #Computational chemistry #Core (optical fiber) #Chemical physics #Crystallography #Molecule #Organic chemistry

paper · doi:10.1021/ja044607h

openalex publication_date 2005/02/05 · openalex created_date 2025/10/10 · openalex updated_date 2026/06/26

Abstract

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.

Citations

• Electronic structure calculations on workstation computers: The program system turbomole
• Note on an Approximation Treatment for Many-Electron Systems

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