High stability of a ferredoxin from the hyperthermophilic archaeon A. ambivalens: Involvement of electrostatic interactions and cofactors

Protein Science

Volumn 10, Issue 8, 2001, Pages 1539-1548

  Moczygemba, Charmaine ^a   Guidry, Jesse ^a   Jones, Kathryn L ^b   Gomes, Cláudio M ^c   Teixeira, Miguel ^c   Wittung Stafshede, Pernilla ^a,b  

^a Tulane University   (United States)

^b TULANE UNIVERSITY   (United States)

^c INSTITUTO DE TECNOLOGIA QUÍMICA E BIOLÓGICA   (Portugal)

Author keywords

Hyperthermophiles; Iron sulfur proteins; Protein unfolding; Thermostability

Indexed keywords

FERREDOXIN; GUANIDINE; IRON SULFUR PROTEIN;

ACIDIANUS AMBIVALENS; ARTICLE; ELECTRICITY; ENTHALPY; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; REACTION ANALYSIS; TEMPERATURE DEPENDENCE; THERMOSTABILITY;

ARCHAEAL PROTEINS; CIRCULAR DICHROISM; DISINFECTANTS; ELECTROSTATICS; FERREDOXINS; GUANIDINE; GUANIDINES; HYDROGEN-ION CONCENTRATION; IRON; MODELS, MOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; SULFOLOBACEAE; SULFUR; TEMPERATURE; THERMODYNAMICS; THIOCYANATES; ZINC;

ACIDIANUS AMBIVALENS; ARCHAEA;

EID: 0034926051     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.49401     Document Type: Article

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