Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands

Protein Science

Volumn 5, Issue 9, 1996, Pages 1844-1851

  Uversky, Vladimir N ^a   Kutyshenko, Viktor P ^b   Protasova, Natalya Yu ^a   Rogov, Vladimir V ^a   Vassilenko, Konstantin S ^a   Gudkov, Anatoly T ^a  

^a INSTITUTE OF PROTEIN RESEARCH   (Russian Federation)

^b INSTITUTE OF THEORETICAL AND EXPERIMENTAL BIOPHYSICS   (Russian Federation)

Author keywords

circular permutation; conformational changes; dihydrofolate reductase; molten globule; protein folding and stability

Indexed keywords

DIHYDROFOLATE REDUCTASE;

AMINO ACID SEQUENCE; ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; STRUCTURE ACTIVITY RELATION;

EID: 0029786618     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050910     Document Type: Article

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