%0 Journal Article %1 Seo2014OpeningRateLigandDissociation %A Seo, Moon-Hyeong %A Park, Jeongbin %A Kim, Eunkyung %A Hohng, Sungchul %A Kim, Hak-Sung %D 2014 %I Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. %J Nat Commun %K conformational-changes ligand-binding ligand-dissociation opening-rate %T Protein conformational dynamics dictate the binding affinity for a ligand %U http://dx.doi.org/10.1038/ncomms4724 %V 5 %X Interactions between a protein and a ligand are essential to all biological processes. Binding and dissociation are the two fundamental steps of ligand–protein interactions, and determine the binding affinity. Intrinsic conformational dynamics of proteins have been suggested to play crucial roles in ligand binding and dissociation. Here, we demonstrate how protein dynamics dictate the binding and dissociation of a ligand through a single-molecule kinetic analysis for a series of maltose-binding protein mutants that have different intrinsic conformational dynamics and dissociation constants for maltose. Our results provide direct evidence that the ligand dissociation is determined by the intrinsic opening rate of the protein.

@article{Seo2014OpeningRateLigandDissociation, abstract = {Interactions between a protein and a ligand are essential to all biological processes. Binding and dissociation are the two fundamental steps of ligand–protein interactions, and determine the binding affinity. Intrinsic conformational dynamics of proteins have been suggested to play crucial roles in ligand binding and dissociation. Here, we demonstrate how protein dynamics dictate the binding and dissociation of a ligand through a single-molecule kinetic analysis for a series of maltose-binding protein mutants that have different intrinsic conformational dynamics and dissociation constants for maltose. Our results provide direct evidence that the ligand dissociation is determined by the intrinsic opening rate of the protein.}, added-at = {2016-03-07T22:10:26.000+0100}, author = {Seo, Moon-Hyeong and Park, Jeongbin and Kim, Eunkyung and Hohng, Sungchul and Kim, Hak-Sung}, biburl = {https://www.bibsonomy.org/bibtex/2faefd70145aca078a97045d2db0fee4e/salotz}, comment = {Supplementary information available for this article at http://www.nature.com/ncomms/2014/140424/ncomms4724/suppinfo/ncomms4724_S1.html}, description = {Protein conformational dynamics dictate the binding affinity for a ligand : Nature Communications : Nature Publishing Group}, interhash = {fd289750e481b3c9b964234a2e3c0864}, intrahash = {faefd70145aca078a97045d2db0fee4e}, journal = {Nat Commun}, keywords = {conformational-changes ligand-binding ligand-dissociation opening-rate}, month = apr, publisher = {Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.}, timestamp = {2016-03-07T22:10:26.000+0100}, title = {Protein conformational dynamics dictate the binding affinity for a ligand}, url = {http://dx.doi.org/10.1038/ncomms4724}, volume = 5, year = 2014 }