Pretransitional Structural Changes in the Thermal Denaturation of Ribonuclease S and S Protein
نویسندگان
چکیده
منابع مشابه
A study of the thermal denaturation of ribonuclease S by electrospray ionization mass spectrometry.
The thermal stability of ribonuclease S (RNase S), an enzymatically active noncovalent complex composed of a 2166-u peptide (S-peptide) and a 11,534-u protein (S-protein), was investigated by electrospray ionization mass spectrometry (ESI-MS) and capillary electrophoresis ESI-MS (CE-ESI-MS). The intensities of peaks corresponding to the RNase S complex were inversely related to both the applied...
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The thermal denaturation of ribonuclease A and of S-protein in neutral aqueous solutions has been studied by means of their circular dichroism spectra. For RNase A, the positive circular dichroism extremum near 241 rnp shows a biphasic dependence upon temperature, a linear change between 15” and 50” being followed by a sharp one above 52”. The negative circular dichroism extremum at 277 rnp exh...
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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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The S-peptide and S-protein fragments of ribonuclease S (RNase S, no EC no. assigned) have been immobilized onto separate Sepharose gels via a "leash" of polycytidylic acid substrate. Each of these gels releases its RNase fragment when treated with the complementary enzyme fragment or with RNase A (EC 3.1.27.5), and the released fragments recombine to give RNase S activity. Thus this system pro...
متن کاملStructural and thermodynamic consequences of introducing alpha-aminoisobutyric acid in the S peptide of ribonuclease S.
The S protein-S peptide interaction is a model system to study binding thermodynamics in proteins. We substituted alanine at position 4 in S peptide by alpha-aminoisobutyric acid (Aib) to investigate the effect of this substitution on the conformation of free S peptide and on its binding to S protein. The thermodynamic consequences of this replacement were studied using isothermal titration cal...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2002
ISSN: 0006-3495
DOI: 10.1016/s0006-3495(02)73986-6