The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate

Protein Science

Volumn 7, Issue 11, 1998, Pages 2331-2344

  Van Mierlo, Carlo P M ^a   Van Dongen, Walter M A M ^a   Vergeldt, Frank ^a   Van Berkel, Willem J H ^a   Steensma, Elles ^a  

^a WAGENINGEN UNIVERSITY   (Netherlands)

Author keywords

Apoflavodoxin; Circular dichroism; Equilibrium unfolding; Fluorescence; Molten globule like species; NMR; Protein stability; Three state model

Indexed keywords

APOFLAVODOXIN; DEUTERIUM; FLAVINE MONONUCLEOTIDE; FLAVODOXIN; HYDROGEN; UNCLASSIFIED DRUG;

ARTICLE; AZOTOBACTER VINELANDII; FLUORESCENCE SPECTROSCOPY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY;

AZOTOBACTER VINELANDII; BACTERIA (MICROORGANISMS);

EID: 0031792027     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560071110     Document Type: Article

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