Calmodulin Conformational Binding Entropy Is Driven by Transient Salt Bridges
نویسندگان
چکیده
منابع مشابه
The role of conformational entropy in molecular recognition by calmodulin
The physical basis for high-affinity interactions involving proteins is complex and potentially involves a range of energetic contributions. Among these are changes in protein conformational entropy, which cannot yet be reliably computed from molecular structures. We have recently used changes in conformational dynamics as a proxy for changes in conformational entropy of calmodulin upon associa...
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A similar error occurs in the figure legend for Supplementary Fig. 16. The figure legend should read: ‘Supplementary Fig. 16: Distribution of simulated trajectory lengths. For the (a) apo and (b) holo CaM systems, 12,184 and 9,995 trajectories were simulated for a total time of 256 and 455 ms, respectively. Trajectories shorter than the lag time at which the MSMs were built were eliminated from...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2012
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2011.11.368