title: Energetic Calculations to Decipher pH-Dependent Oligomerization and Domain Swapping of Proteins.
abstract: Domain swapping mechanism is a specialised mode of oligomerization of proteins in which part of a protein is exchanged in a non-covalent manner between constituent subunits. This mechanism is highly affected by several physiological conditions. Here, we present a detailed analysis ofthe effect of pH on different regions of the domain swapped oligomer by considering examples which are known to be sensitive to pH in transiting from monomeric to domain-swapped dimeric form. The energetic calculations were performed using a specialized method which considers changes in pH and subsequent changes in the interactions between subunits. This analysis provides definitive hints about the pH-dependence switch from monomer to domain-swapped oligomer and the steps that may be involved in the swapping mechanism.
authors.affiliation: National Centre for Biological Sciences, GKVK Campus, Bellary Road, Bangalore, 560065, India.
authors.forename: Prashant
authors.initials: P
authors.lastname: Shingate
authors.affiliation: Faculty of Life Sciences, John Garside Building (MIB), 131 Princess Street, Manchester, M1 7DN, University of Manchester, Manchester, United Kingdom.
authors.forename: Jim
authors.initials: J
authors.lastname: Warwicker
authors.affiliation: National Centre for Biological Sciences, GKVK Campus, Bellary Road, Bangalore, 560065, India.
authors.forename: Ramanathan
authors.initials: R
authors.lastname: Sowdhamini
mesh_terms: D030562:Databases, Protein; D008956:Models, Chemical; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000235:genetics
chemical_list: D011506:Proteins