The effect of net charge on the solubility, activity, and stability of ribonuclease Sa

Protein Science

Volumn 10, Issue 6, 2001, Pages 1206-1215

  Shaw, Kevin L ^a,d   Grimsley, Gerald R ^a   Yakovlev, Gennady I ^b   Makarov, Alexander A ^b   Pace, C Nick ^a,c  

^a TEXAS A M COLLEGE OF MEDICINE   (United States)

^b ENGELHARDT INSTITUTE OF MOLECULAR BIOLOGY   (Russian Federation)

^c TEXAS A AND M UNIVERSITY   (United States)

^d GROVE CITY COLLEGE   (United States)

Author keywords

Electrostatic interactions; Enzyme activity; Isoelectric pH; Net charge; Protein solubility; Protein stability; Ribonuclease Sa

Indexed keywords

RIBONUCLEASE;

ARTICLE; CONFORMATIONAL TRANSITION; ELECTRICITY; ENZYME ACTIVITY; ENZYME STABILITY; HYDROGEN BOND; ISOELECTRIC POINT; PRIORITY JOURNAL; RESIDUE ANALYSIS; SOLUBILITY; THERMODYNAMICS;

ASPARTIC ACID; CIRCULAR DICHROISM; ESCHERICHIA COLI; GLUTAMIC ACID; HYDROGEN-ION CONCENTRATION; ISOENZYMES; KINETICS; LYSINE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN DENATURATION; RIBONUCLEASES; SOLUBILITY; TEMPERATURE; THERMODYNAMICS;

EID: 0035009229     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.440101     Document Type: Article

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