Extreme Free Energy Stabilization of Taq DNA Polymerase

Proteins: Structure, Function and Genetics

Volumn 54, Issue 4, 2004, Pages 616-621

  Schoeffler, Allyn J ^a   Joubert, Allison M ^a   Peng, Fenggang ^a   Khan, Farheen ^a   Liu, Chin Chi ^a   LiCata, Vince J ^a  

^a LOUISIANA STATE UNIVERSITY   (United States)

Author keywords

Chemical denaturation; Klenow polymerase; Protein unfolding; Sedimentation coefficient; Taq polymerase; Thermophilic

Indexed keywords

DNA DIRECTED DNA POLYMERASE BETA; DNA FRAGMENT; GUANIDINE; MONOMER; TAQ POLYMERASE;

ARTICLE; DENATURATION; ENERGY; ESCHERICHIA COLI; HIGH TEMPERATURE; NONHUMAN; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN STABILITY; SEDIMENTATION; THERMODYNAMICS; THERMUS AQUATICUS;

DNA POLYMERASE I; ENZYME STABILITY; ESCHERICHIA COLI; GUANIDINE; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; TAQ POLYMERASE; THERMODYNAMICS; THERMUS;

ESCHERICHIA COLI; THERMUS AQUATICUS;

EID: 1542286214     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10641     Document Type: Article

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