What determines the strength of noncovalent association of ligands to proteins in aqueous solution?
basic_science · Level V
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- Record sourced from PubMed, PMID 8378312.
- Also identified by PMC identifier 47364.
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Abstract
Free energy perturbation methods using molecular dynamics have been used to calculate the absolute free energy of association of two ligand-protein complexes. The calculations reproduce the significantly more negative free energy of association of biotin to streptavidin, compared to N-L-acetyltryptophanamide/alpha-chymotrypsin. This difference in free energy of association is due to van der Waals/dispersion effects in the nearly ideally performed cavity that streptavidin presents to biotin, which involves four tryptophan residues.
Medical subject headings
- Bacterial Proteins
- Chymotrypsin
- Ligands
- Proteins