An inserted Gly residue fine tunes dynamics between mesophilic and thermophilic ribonucleases H

Protein Science

Volumn 15, Issue 12, 2006, Pages 2697-2707

  Butterwick, Joel A ^a,b   Palmer III, Arthur G ^a  

^a Och Spine at New York Presbyterian Hospitals   (United States)

^b ROCKEFELLER UNIVERSITY   (United States)

Author keywords

Nuclear magnetic resonance; Protein dynamics; Ribonuclease H; Thermal stability

Indexed keywords

GLYCINE; RIBONUCLEASE H;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; CONFORMATIONAL TRANSITION; DYNAMICS; ESCHERICHIA COLI; HYDROGEN BOND; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; RESIDUE ANALYSIS; TEMPERATURE; THERMODYNAMICS; THERMOSTABILITY; THERMUS THERMOPHILUS;

AMINO ACID SEQUENCE; ESCHERICHIA COLI; GLYCINE; ION EXCHANGE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, INSERTIONAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RIBONUCLEASE H, CALF THYMUS; SEQUENCE HOMOLOGY, AMINO ACID; TEMPERATURE; THERMODYNAMICS; THERMUS THERMOPHILUS;

ESCHERICHIA COLI; THERMUS THERMOPHILUS;

EID: 33751513293     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062398606     Document Type: Article

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