Asp79 makes a large, unfavorable contribution to the stability of RNase Sa

Journal of Molecular Biology

Volumn 354, Issue 4, 2005, Pages 967-978

  Trevino, Saul R ^a   Gokulan, Kuppan ^b   Newsom, Stephanie ^a,e   Thurlkill, Richard L ^b   Shaw, Kevin L ^b,f   Mitkevich, Vladimir A ^c,d   Makarov, Alexander A ^c   Sacchettini, James C ^b   Scholtz, J Martin ^a,b   Pace, C Nick ^a,b  

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

^b TEXAS A AND M UNIVERSITY   (United States)

^c ENGELHARDT INSTITUTE OF MOLECULAR BIOLOGY   (Russian Federation)

^d UNIVERSITY OF OSLO   (Norway)

^e UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^f GROVE CITY COLLEGE   (United States)

Author keywords

Buried carboxyl group; Hydrogen bonds; Ion pair; pK; Protein stability

Indexed keywords

ASPARTIC ACID; CARBOXYL GROUP; HYDROGEN; RIBONUCLEASE; UNCLASSIFIED DRUG;

ACIDITY; ALKALINITY; ARTICLE; CRYSTAL STRUCTURE; ELECTRICITY; ENERGY; ENZYME STABILITY; GENETIC STRAIN; GENETIC VARIABILITY; HYDROGEN BOND; HYDROPHOBICITY; IONIZATION; OBSERVATION; PRIORITY JOURNAL; PROTEIN STABILITY; RIBONUCLEASE SA; STEREOSPECIFICITY; WILD TYPE;

EID: 28444469414     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.09.091     Document Type: Article

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