Intramolecular interactions at protein surfaces and their impact on protein function.
Protein surfaces play a key role in the biological function of proteins. Consequently, structural features of protein surfaces are the basis for predicting function from structure. A well-established principle of binding by proteins is that ligands must compete with water and other small molecules to form interactions with protein surfaces. A less obvious issue, and the emphasis of this article, is that ligands must also compete with interactions among residues at protein surfaces. Results from structural surveys, a variety of experimental studies and computations suggest that intramolecular interactions are present at protein surfaces and that the energetics of these interactions can change when proteins bind to other molecules.
D000818:Animals; D001665:Binding Sites; D006801:Humans; D006860:Hydrogen Bonding; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D055672:Static Electricity; D013499:Surface Properties; D013816:Thermodynamics
D011506:Proteins