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Updated: Jun 25, 2026

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
Published on: April 28, 2011
Analysis of oligomeric proteins during unfolding by pH and temperature
Pradip Bhattacharya1, Tamil Ganeshan, Soumiyadeep Nandi
1School of Life Sciences, Jawaharlal Nehru University, New Delhi, 110067, India. pradip.bhattacharya13@gmail.com
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.
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