Dissimilar roles of the four conserved acidic residues in the thermal stability of poly(A)-specific ribonuclease

International Journal of Molecular Sciences

Volumn 12, Issue 5, 2011, Pages 2901-2916

  He, Guang Jun ^a   Liu, Wei Feng ^a   Yan, Yong Bin ^a  

^a TSINGHUA UNIVERSITY   (China)

Author keywords

Aggregation kinetics; Magnesium ions; Poly(A) specific ribonuclease (PARN); Structural stability; Thermal aggregation; Two metal ion catalysis

Indexed keywords

MAGNESIUM ION; POLYADENYLIC ACID; POLYADENYLIC ACID SPECIFIC RIBONUCLEASE; RIBONUCLEASE; UNCLASSIFIED DRUG; EXORIBONUCLEASE; MAGNESIUM; POLY(A)-SPECIFIC RIBONUCLEASE;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME STRUCTURE; METAL BINDING; MUTATIONAL ANALYSIS; PROTEIN AGGREGATION; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; THERMOSTABILITY; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; KINETICS; MUTATION; NUCLEOTIDE SEQUENCE; PROTEIN STABILITY; SITE DIRECTED MUTAGENESIS;

CATALYTIC DOMAIN; CONSERVED SEQUENCE; EXORIBONUCLEASES; KINETICS; MAGNESIUM; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN STABILITY;

EID: 79957830763     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms12052901     Document Type: Article

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