Conformational stability and thermodynamic characterization of the lipoic acid bearing domain of human mitochondrial branched chain α-ketoacid dehydrogenase

Protein Science

Volumn 13, Issue 9, 2004, Pages 2483-2492

  Naik, Mandar T ^a   Huang, Tai Huang ^a,b  

^a INSTITUTE OF BIOMEDICAL SCIENCES   (Taiwan)

^b NATIONAL TAIWAN NORMAL UNIVERSITY   (Taiwan)

Author keywords

BCKD; Branched chain keto acid dehydrogenase; hbLBD; Lipoic acid bearing domain; Maple syrup urine disease; MSUD; Protein conformational stability

Indexed keywords

2 OXOISOVALERATE DEHYDROGENASE (LIPOAMIDE); MITOCHONDRIAL ENZYME; THIOCTIC ACID; UREA;

ARTICLE; COLD DENATURATION; COLD EXPOSURE; CONFORMATIONAL TRANSITION; DECARBOXYLATION; KINETIC INTERMEDIATE; MAPLE SYRUP URINE DISEASE; NONHUMAN; OXIDATION; OXIDATIVE DECARBOXYLATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; THERMODYNAMICS; THERMOSTABILITY;

3-METHYL-2-OXOBUTANOATE DEHYDROGENASE (LIPOAMIDE); CIRCULAR DICHROISM; ENZYME STABILITY; HUMANS; LINEAR MODELS; MITOCHONDRIA; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, TERTIARY; THERMODYNAMICS; THIOCTIC ACID; ULTRAVIOLET RAYS; UREA;

ACER;

EID: 4344622456     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.04783104     Document Type: Article

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