Prediction of indirect interactions in proteins

Background: Both direct and indirect interactions determine molecular recognition of ligands by proteins. Indirect interactions can be defined as effects on recognition controlled from distant sites in the proteins, e.g. by changes in protein conformation and mobility, whereas direct interactions occur in close proximity of the protein's amino acids and the ligand. Molecular recognition is traditionally studied using three-dimensional methods, but with such techniques it is difficult to predict the effects caused by mutational changes of amino acids located far away from the ligandbinding site. We recently developed an approach, proteochemometrics, to the study of molecular recognition that models the chemical effects involved in the recognition of ligands by proteins using statistical sampling and mathematical modelling. Results: A proteochemometric model was built, based on a statistically designed protein library's (melanocortin receptors') interaction with three pep...

• Type: Journal
• Year: 2006
• Where: BMCBI
• Authors: Peteris Prusis, Staffan Uhlén, Ramona Petrovska, Maris Lapinsh, Jarl E. S. Wikberg
• Keywords: BMCBI 2006, Ligand, Molecular Recognition, Protein