Identification of residual structure in the unfolded state of ribonuclease H1 from the moderately thermophilic chlorobium tepidum: Comparison with thermophilic and mesophilic homologues

Biochemistry

Volumn 49, Issue 25, 2010, Pages 5167-5175

  Ratcliff, Kathleen ^a,b   Marqusee, Susan ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHIMERIC PROTEINS; COMPUTATIONAL INVESTIGATION; CORE REGION; HEAT CAPACITIES; HIGHER TEMPERATURES; HYDROPHOBIC RESIDUES; MESOPHILES; MESOPHILIC; MODERATELY THERMOPHILIC; RESIDUAL STRUCTURE; RNASE H; THERMOPHILIC PROTEINS; THERMOPHILUS; THERMUS THERMOPHILUS; VARIABLE CHANGE;

BIOCHEMISTRY; HYDROPHOBICITY;

PROTEINS;

CHIMERIC PROTEIN; RIBONUCLEASE H;

AMINO ACID SEQUENCE; ARTICLE; CHLOROBIUM TEPIDUM; CONTROLLED STUDY; ENZYME STRUCTURE; HYDROPHOBICITY; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; THERMODYNAMICS; THERMOPHILIC BACTERIUM;

CHLOROBIUM; GENES, BACTERIAL; MUTAGENESIS; PROTEIN CONFORMATION; PROTEIN DENATURATION; RIBONUCLEASE H; THERMODYNAMICS;

CHLOROBACULUM TEPIDUM; THERMUS THERMOPHILUS;

EID: 77953905699     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1001097     Document Type: Article

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