Analysis of oligomeric proteins during unfolding by pH and temperature |
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| Authors: | Pradip Bhattacharya Tamil Ganeshan Soumiyadeep Nandi Alok Srivastava Prashant Singh Mohommad Rehan Reshmi Rashkush Naidu Subbarao Andrew Lynn |
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| Institution: | (1) School of Life Sciences, Jawaharlal Nehru University, New Delhi, 110067, India;(2) School of Information Technology, Jawaharlal Nehru University, New Delhi, 110067, India |
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| 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.
Electronic supplementary material The online version of this article (doi:) contains supplementary material, which is available to authorized users. |
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| Keywords: | Analysis of structure and conformation at various pH Binding free energy Docking Electrostatic charge of protein Free energy Molecular dynamic simulation Oligomeric proteins Unfolding of proteins Variation of pH and temperature |
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