An alternate conformation of the hyperthermostable HU protein from Thermotoga maritima has unexpectedly high flexibility

FEBS Letters

Volumn 563, Issue 1-3, 2004, Pages 49-54

  Durney, Michael A ^a,b   Wechselberger, Rainer W ^a   Kalodimos, Charalampos G ^a,d   Kaptein, Robert ^a   Vorgias, Constantinos E ^c   Boelens, Rolf ^a  

^a UTRECHT UNIVERSITY   (Netherlands)

^b UNIVERSITY OF SOUTHAMPTON   (United Kingdom)

^c UNIVERSITY OF ATHENS   (Greece)

^d RUTGERS UNIVERSITY   (United States)

Author keywords

Conformational flexibility; HUBst, Bacillus stearothermophilus HU protein; HUBsu, Bacillus subtilis HU protein; HUTmar, Thermotoga maritima HU protein; Nuclear magnetic resonance spin relaxation; Protein dynamics; Thermostability

Indexed keywords

HU PROTEIN; HYDROGEN;

ARTICLE; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; THERMOSTABILITY; THERMOTOGA MARITIMA; X RAY ANALYSIS;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; DRUG STABILITY; HEAT; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PLIABILITY; POINT MUTATION; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID; SOLUTIONS; THERMOTOGA MARITIMA;

BACILLUS SUBTILIS; GEOBACILLUS STEAROTHERMOPHILUS; THERMOTOGA; THERMOTOGA MARITIMA;

EID: 1842788231     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(04)00247-9     Document Type: Article

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