Pathways for Conformational Change in Nitrogen Regulatory Protein C from Discrete Path Sampling Export

@article{citeulike:5041213, abstract = {PMID: 18247595 Pathways corresponding to the conformational change in nitrogen regulatory protein C are calculated using the CHARMM19 force field with an implicit solvation model. Our analysis employs the discrete path sampling approach to grow a database of local minima and transition states from the potential energy surface that contains kinetically relevant pathways. The pathways with the largest contribution to the phenomenological two-state rate constants are found to exhibit a number of structural features that agree with experimental observations. Further details of the calculated pathways for conformational change may therefore provide useful predictions of how this large-scale motion is achieved.}, author = {Khalili, Mey and Wales, David J.}, citeulike-article-id = {5041213}, citeulike-linkout-0 = {http://dx.doi.org/10.1021/jp076628e}, citeulike-linkout-1 = {http://pubs.acs.org/doi/abs/10.1021/jp076628e}, day = {1}, doi = {10.1021/jp076628e}, journal = {The Journal of Physical Chemistry B}, keywords = {first\_passage, free-energy, protein\_dynamics, qha, reaction\_paths, transition\_path, transition\_states}, month = {February}, number = {8}, pages = {2456--2465}, posted-at = {2009-07-02 12:02:29}, priority = {2}, title = {Pathways for Conformational Change in Nitrogen Regulatory Protein C from Discrete Path Sampling}, url = {http://dx.doi.org/10.1021/jp076628e}, volume = {112}, year = {2008} }

TY - JOUR ID - citeulike:5041213 L3 - citeulike-article-id:5041213 N2 - PMID: 18247595 Pathways corresponding to the conformational change in nitrogen regulatory protein C are calculated using the CHARMM19 force field with an implicit solvation model. Our analysis employs the discrete path sampling approach to grow a database of local minima and transition states from the potential energy surface that contains kinetically relevant pathways. The pathways with the largest contribution to the phenomenological two-state rate constants are found to exhibit a number of structural features that agree with experimental observations. Further details of the calculated pathways for conformational change may therefore provide useful predictions of how this large-scale motion is achieved. IS - 8 JF - The Journal of Physical Chemistry B EP - 2465 TI - Pathways for Conformational Change in Nitrogen Regulatory Protein C from Discrete Path Sampling VL - 112 SP - 2456 KW - first_passage KW - free-energy KW - protein_dynamics KW - qha KW - reaction_paths KW - transition_path KW - transition_states AU - Khalili, Mey AU - Wales, David PY - 2008/02/01/ UR - http://dx.doi.org/10.1021/jp076628e ER -