Conformational Contribution to Thermodynamics of Binding in Protein-Peptide Complexes through Microscopic Simulation

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• 作者：Amit Das^&dagger ; ; J. Chakrabarti^&dagger ; ; ^&Dagger ; ; ^{jaydeb@bose.res.in} ; Mahua Ghosh^&dagger ; ; ^{mahuaghosh@bose.res.in}
• 刊名：Biophysical Journal
• 出版年：2013
• 出版时间：19 March, 2013
• 年：2013
• 卷：104
• 期：6
• 页码：1274-1284
• 全文大小：747 K

文摘

We extract the thermodynamics of conformational changes in biomacromolecular complexes from the distributions of the dihedral angles of the macromolecules. These distributions are obtained from the equilibrium configurations generated via all-atom molecular dynamics simulations. The conformational thermodynamics data we obtained for calmodulin-peptide complexes using our methodology corroborate well with the experimentally observed conformational and binding entropies. The conformational free-energy changes and their contributions for different peptide-binding regions of calmodulin are evaluated microscopically.