New Thermodynamic Studies on Ribonuclease A at Low pH
نویسندگان
چکیده
منابع مشابه
Studies on Ribonuclease S
Specific regions of the polypeptide sequence of pancreatic ribonuclease have been altered by chemical modification and by limited proteolytic digestion in attempts to implicate specific covalent portions of the molecule in the structure and stabilization of the active center. Digestion of the native molecule with trypsin at elevated temperatures has been shown to remove portions of the chain wi...
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Tryptophan was substituted for Tyr92 to create a sensitive and unique optical probe in order to study the unfolding and refolding kinetics of disulfide-intact bovine pancreatic ribonuclease A by fluorescence-detected stopped-flow techniques. The stability of the Trp mutant was found to be similar to that of wild-type RNase A when denatured by heat or GdnHCl, and the mutant was found to have 85%...
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The thermal denaturation of ribonuclease A has been studied by use of Fourier transform nuclear magnetic resonance by monitoring the imidazole C-2 proton resonances of the histidine residues as a function of temperature at pH 1.3. As the temperature is raised, a slow chemical exchange process results in the disappearance of the peaks corresponding to the native conformation and the appearance o...
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Alkali-denatured bovine pancreatic ribonuclease (RNase) reacts poorly with antibody to the native molecule, and RNase whose disulfide bridges have been broken by oxidation or reduction is completely inactive with this antiserum. These observations suggest that the antigenicity of the native protein is, in part, attributable to its conformation (1). Oxidized RNase has no detectable immunogenic o...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1995
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)48646-7