Structural and thermal stability analysis of Escherichia coli and Alicyclobacillus acidocaldarius thioredoxin revealed a molten globule-like state in thermal denaturation pathway of the proteins: An infrared spectroscopic study

Biochemical Journal

Volumn 373, Issue 3, 2003, Pages 875-883

  Pedone, Emilia ^a   Bartolucci, Simonetta ^b   Rossi, Mosè ^b,c   Pierfederici, Francesco Maria ^d   Scirè, Andrea ^e   Cacciamani, Tiziana ^e   Tanfani, Fabio ^e  

^a CNR   (Italy)

^b UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^c INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

^d UNIVERSITY OF CATANIA   (Italy)

^e UNIVERSITÀ POLITECNICA DELLE MARCHE   (Italy)

Author keywords

Fourier transform IR (FTIR) spectroscopy; Molten globule like state; Protein aggregation; Thermostability; Thioredoxin; Two dimensional IR correlation analysis

Indexed keywords

ESCHERICHIA COLI; FOURIER TRANSFORM INFRARED SPECTROSCOPY; MOLECULAR STRUCTURE; PROTEINS; THERMODYNAMIC STABILITY;

MUTANTS;

BIOCHEMISTRY;

BACTERIAL PROTEIN; THIOREDOXIN;

ALICYCLOBACILLUS ACIDOCALDARIUS; ANALYTIC METHOD; ARTICLE; BACTERIUM; CONTROLLED STUDY; ESCHERICHIA COLI; INFRARED SPECTROSCOPY; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN STRUCTURE; TEMPERATURE DEPENDENCE; THERMOSTABILITY;

ENZYME STABILITY; ESCHERICHIA COLI; PROTEIN CONFORMATION; PROTEIN DENATURATION; SPECTROPHOTOMETRY, INFRARED; THIOREDOXIN;

ALICYCLOBACILLUS; ALICYCLOBACILLUS ACIDOCALDARIUS; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0043069834     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021747     Document Type: Article

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