Analysis of oligomeric proteins during unfolding by pH and temperature.
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.
Bhattacharya
Pradip
P
School of Life Sciences, Jawaharlal Nehru University, New Delhi, 110067, India. pradip.bhattacharya13@gmail.com
Ganeshan
Tamil
T
Nandi
Soumiyadeep
S
Srivastava
Alok
A
Singh
Prashant
P
Rehan
Mohommad
M
Rashkush
Reshmi
R
Subbarao
Naidu
N
Lynn
Andrew
A
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
D011506:Proteins