Abstract:
:Using the binding of a nucleotide inhibitor (guanosine-3'-monophosphate) to a ribonuclease (ribonuclease Sa) as a model system, we show that the salt-dependence of the interaction arises due to specific ion binding at the site of nucleotide binding. The presence of specific ion-protein binding is concluded from a combination of differential scanning calorimetry and NMR data. Isothermal titration calorimetry data are then fit to determine the energetic profile (enthalpy, entropy, and heat capacity) for both the ion-protein and nucleotide-protein interactions. The results provide insight into the energetics of charge-charge interactions, and have implications for the interpretation of an observed salt-dependence. Further, the presence of specific ion-binding leads to a system behavior as a function of temperature that is drastically different from that predicted from Poisson-Boltzmann calculations.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Waldron TT,Schrift GL,Murphy KPdoi
10.1016/j.jmb.2004.12.018keywords:
subject
Has Abstractpub_date
2005-02-25 00:00:00pages
895-905issue
3eissn
0022-2836issn
1089-8638pii
S0022-2836(04)01588-8journal_volume
346pub_type
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