Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR

To understand the process of protein folding, it will be necessary to obtain detailed structural information on folding intermediates. This difficult problem is being studied by using hydrogen exchange and rapid mixing to label transient structural intermediates, with subsequent analysis of the prot...

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Bibliographic Details
Published inNature (London) Vol. 335; no. 6192; p. 700
Main Authors Roder, H, Elöve, G A, Englander, S W
Format Journal Article
LanguageEnglish
Published England 20.10.1988
Subjects
Cytochrome c Group
Kinetics
Magnetic Resonance Spectroscopy
Models, Molecular
Protein Conformation
Protons
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Summary:To understand the process of protein folding, it will be necessary to obtain detailed structural information on folding intermediates. This difficult problem is being studied by using hydrogen exchange and rapid mixing to label transient structural intermediates, with subsequent analysis of the proton-labelling pattern by two-dimensional nuclear magnetic resonance spectroscopy. Results for cytochrome c show that the method provides the spatial and temporal resolution necessary to monitor structure formation at many defined sites along the polypeptide chain on a timescale ranging from milliseconds to minutes.
ISSN:0028-0836
DOI:10.1038/335700a0