title: Analysis of oligomeric proteins during unfolding by pH and temperature.
abstract: During thermal transition and variation of pH, structural properties of 35 proteins and their complexes (bound with substrate and co-factor) were analyzed in detail. During pH alteration, these proteins were shown to have substantial differences in conformations. pH conformers were analyzed in detail. Free energy and other energy parameters were also estimated for these proteins at various pH and temperatures. Detailed structural analysis and binding interfaces of various substrates, inhibitors and cofactor of these proteins were also investigated using docking and molecular dynamic simulation.
authors.affiliation: School of Life Sciences, Jawaharlal Nehru University, New Delhi, 110067, India. pradip.bhattacharya13@gmail.com
authors.forename: Pradip
authors.initials: P
authors.lastname: Bhattacharya
authors.forename: Tamil
authors.initials: T
authors.lastname: Ganeshan
authors.forename: Soumiyadeep
authors.initials: S
authors.lastname: Nandi
authors.forename: Alok
authors.initials: A
authors.lastname: Srivastava
authors.forename: Prashant
authors.initials: P
authors.lastname: Singh
authors.forename: Mohommad
authors.initials: M
authors.lastname: Rehan
authors.forename: Reshmi
authors.initials: R
authors.lastname: Rashkush
authors.forename: Naidu
authors.initials: N
authors.lastname: Subbarao
authors.forename: Andrew
authors.initials: A
authors.lastname: Lynn
mesh_terms: D000818:Animals; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013696:Temperature; D013816:Thermodynamics
chemical_list: D011506:Proteins