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Article: New physical chemistry findings from K. Berka and co-authors described.
- Article from:
- Chemicals & Chemistry
- Article date:
- May 1, 2009
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According to a study from Prague, Czech Republic, "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. The results show uniform ...