Literature DB >> 19205760

Analysis of oligomeric proteins during unfolding by pH and temperature.

Pradip Bhattacharya1, Tamil Ganeshan, Soumiyadeep Nandi, Alok Srivastava, Prashant Singh, Mohommad Rehan, Reshmi Rashkush, Naidu Subbarao, Andrew Lynn.   

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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Year:  2009        PMID： 19205760     DOI： 10.1007/s00894-008-0365-1

Source DB:  PubMed          Journal:  J Mol Model        ISSN： 0948-5023            Impact factor:   1.810


  72 in total

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  1 in total

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  1 in total

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