The stability of Taq DNA polymerase results from a reduced entropic folding penalty; identification of other thermophilic proteins with similar folding thermodynamics

Proteins: Structure, Function and Bioinformatics

Volumn 82, Issue 5, 2014, Pages 785-793

  Liu, Chin Chi ^a   LiCata, Vince J ^a  

^a LOUISIANA STATE UNIVERSITY   (United States)

Author keywords

Entropic barrier; Gibbs Helmholtz; Heat capacity; Klenow; Protein folding; Taq polymerase

Indexed keywords

DNA POLYMERASE; TAQ POLYMERASE;

ARTICLE; CHLOROBIUM; CHLOROBIUM TEPIDUM; CIRCULAR DICHROISM; CONTROLLED STUDY; ENTHALPY; ENTROPY; HEAT; MESOPHILE; METHANOBACTERIUM FORMICICUM; NONHUMAN; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN UNFOLDING; PYROCOCCUS; TEMPERATURE; THERMOPHILE; THERMOSTABILITY; THERMUS THERMOPHILUS; CHEMISTRY; ENZYME STABILITY; METABOLISM;

ENTROPY; ENZYME STABILITY; PROTEIN DENATURATION; PROTEIN FOLDING; TAQ POLYMERASE; TEMPERATURE;

EID: 84898038119     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24458     Document Type: Article

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