Equilibrium unfolding of RNase Rs from Rhizopus stolonifer: pH dependence of chemical and thermal denaturation

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1648, Issue 1-2, 2003, Pages 184-194

  Deshpande, Rajashree A ^a,b   Khan, M Islam ^a   Shankar, Vepatu ^a  

^a NATIONAL CHEMICAL LABORATORY   (India)

^b UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

Acid, base and thermal denaturation; Aggregation; ANS binding; Hydrophobic and electrostatic interaction; RNase T2 family

Indexed keywords

ALPHA CYCLODEXTRIN; RIBONUCLEASE; RIBONUCLEASE RS; UNCLASSIFIED DRUG; UREA; GUANIDINE;

ARTICLE; CIRCULAR DICHROISM; DENATURATION; ELECTRICITY; FLUORESCENCE; HEAT TREATMENT; HYDROPHOBICITY; MATHEMATICAL COMPUTING; MEASUREMENT; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; NONHUMAN; PH; PRECIPITATION; PRIORITY JOURNAL; PROTEIN FOLDING; RHIZOPUS; RHIZOPUS STOLONIFER; STATISTICAL SIGNIFICANCE; SURFACE PROPERTY; TRANSMISSION ELECTRON MICROSCOPY; CHEMISTRY; ENZYME STABILITY; ENZYMOLOGY; HEAT; METABOLISM; PROTEIN DENATURATION; SPECTROFLUOROMETRY;

ILEX COOKII; RHIZOPUS STOLONIFER;

CIRCULAR DICHROISM; ENZYME STABILITY; GUANIDINE; HEAT; HYDROGEN-ION CONCENTRATION; PROTEIN DENATURATION; PROTEIN FOLDING; RHIZOPUS; RIBONUCLEASES; SPECTROMETRY, FLUORESCENCE; UREA;

EID: 0038644453     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1570-9639(03)00133-X     Document Type: Article

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