This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.The purpose of this experiment was to obtain information about the solvation properties of the protein staphylococcal nuclease in aqueous solution in the presence of different types of cosolvents (glycerol, sorbitol, urea, trifluoroethanol, potassium sulfate) at heat-, cold-, and pressure-induced denaturation conditions using small-angle X-ray scattering. In order to determine the effects of different types of cosolvents on the unfolded states, the measurements included temperature and pressure conditions where unfolding of the proteins sets in (-10 to 70 C and 1 to 6000 bar). In particular the role of hydration and cosolvents on the process of cold denaturation at low temperatures is not understood (experimentally accessible only in the pressure-assisted cold denatured state, e.g., at -10 oC and 1.5 kbar).
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