Abstract
Protein folding and unfolding are crucial for a range of biological phenomena and human diseases. Defining the structural properties of the involved transient species is therefore of prime interest. Using a combination of cold denaturation with NMR spectroscopy, we reveal detailed insight into the unfolding of the homodimeric repressor protein CylR2. Seven three-dimensional structures of CylR2 at temperatures from 25 °C to -16 °C reveal a progressive dissociation of the dimeric protein into a native-like monomeric intermediate followed by transition into a highly dynamic, partially folded state. The core of the partially folded state seems critical for biological function and misfolding.
Publication types
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Research Support, N.I.H., Intramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Binding Sites
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Cold Temperature
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Cytotoxins / chemistry*
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Cytotoxins / genetics
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Cytotoxins / metabolism
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DNA, Bacterial / chemistry*
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DNA, Bacterial / genetics
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DNA, Bacterial / metabolism
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Enterococcus faecalis / genetics
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Enterococcus faecalis / metabolism*
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Escherichia coli / genetics
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Models, Molecular
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Molecular Conformation
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Nuclear Magnetic Resonance, Biomolecular
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Promoter Regions, Genetic
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Protein Binding
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Protein Denaturation
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Protein Folding
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Protein Multimerization
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Protein Unfolding
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
Substances
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Bacterial Proteins
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Cytotoxins
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DNA, Bacterial
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Recombinant Proteins
Associated data
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PDB/2LY
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PDB/2LYJ
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PDB/2LYK
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PDB/2LYL
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PDB/2LYP
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PDB/2LYQ
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PDB/2LYS