Analysis of Energy Stabilization inside the Hydrophobic Core of Rubredoxin

0327972 - ÚOCHB 2010 RIV DE eng J - Journal Article
Berka, Karel - Hobza, Pavel - Vondrášek, Jiří
Analysis of Energy Stabilization inside the Hydrophobic Core of Rubredoxin.
ChemPhysChem. Roč. 10, č. 3 (2009), s. 543-548. ISSN 1439-4235. E-ISSN 1439-7641
R&D Projects: GA ČR GA203/05/0009; GA ČR GA203/06/1727; GA ČR(CZ) GD203/05/H001; GA AV ČR IAA400550510; GA MŠMT LC512
Institutional research plan: CEZ:AV0Z40550506
Keywords : hydrophobic core * protein stability * SAPT method
Subject RIV: CF - Physical ; Theoretical Chemistry
Impact factor: 3.453, year: 2009

The hydrophobic core of globular proteins is responsible for major stabilization of the protein tertiary structure. The prevailing amino-acid residues in the core are of aliphatic or aromatic character, and therefore, the core in a folded protein structure is mostly stabilized by noncovalent interactions of van der Waals origin between the amino-acid side chains. Herein, we present a theoretical analysis of the interaction energy between the amino acids of the hydrophobic core of the small globular protein rubredoxin (Rd) based on the symmetry-adapted perturbation theory (SAPT) method.
Permanent Link: http://hdl.handle.net/11104/0174393