Theoretical and Computational Chemistry

How much entropy is contained in NMR relaxation parameters?



Solution-state NMR relaxation experiments are the cornerstone to study internalprotein dynamics at atomic resolution on time scales that are faster than the overallrotational tumbling time,τR. Since the motions described by NMR relaxation pa-rameters are connected to thermodynamic quantities like conformational entropies, thequestion arises how much of the total entropy is contained within this tumbling time.Using all-atom molecular dynamics (MD) simulations of T4 lysozyme, we found thatentropy build-up is rather fast for the backbone, such that the majority of the entropyis indeed contained in the short-time dynamics. In contrast, the contribution of slowdynamics of side chains on time scales beyondτRon the side chain conformationalentropy is significant and should be taken into account for the extraction of accuratethermodynamic properties.


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