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Volumn 40, Issue 32, 2001, Pages 9579-9586

Effect of the central disulfide bond on the unfolding behavior of elongation factor ts homodimer from thermus thermophilus

(5) Sedlak E a Valusova E a Nesper Brock, M b Antalik M a,c Sprinzl, M b

a P J AFÁRIK UNIVERSITY (Slovakia)

b INSTITUTE OF EXPERIMENTAL PHYSICS (Slovakia)

c UNIVERSITY OF BAYREUTH (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION;

CALORIMETRY; CHEMICAL BONDS; DIMERS; ENTHALPY; MONOMERS; SULFUR; SUPERCONDUCTING TRANSITION TEMPERATURE;

BIOCHEMISTRY;

BACTERIAL PROTEIN; DIMER; ELONGATION FACTOR TS;

ARTICLE; CIRCULAR DICHROISM; CONCENTRATION RESPONSE; DIFFERENTIAL SCANNING CALORIMETRY; DIMERIZATION; DISSOCIATION; DISULFIDE BOND; ENTHALPY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; TEMPERATURE; THERMUS THERMOPHILUS;

BACTERIAL PROTEINS; CALORIMETRY, DIFFERENTIAL SCANNING; DIMERIZATION; DISULFIDES; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; PEPTIDE ELONGATION FACTORS; PERCHLORIC ACID; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SODIUM COMPOUNDS; TEMPERATURE; THERMUS THERMOPHILUS;

BACTERIA (MICROORGANISMS); THERMUS THERMOPHILUS;

EID: 0035859840 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi010274e Document Type: Article

Times cited : (12)

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