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Measuring 1HN temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy.

Bouvignies, G; Vallurupalli, P; Cordes, MHJ; Hansen, DF; Kay, LE; (2011) Measuring 1HN temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy. J Biomol NMR , 50 (1) pp. 13-18. 10.1007/s10858-011-9498-0.

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Abstract

A method based on the Carr-Purcell-Meiboom-Gill relaxation dispersion experiment is presented for measuring the temperature coefficients of amide proton chemical shifts of low populated 'invisible' protein states that exchange with a 'visible' ground state on the millisecond time-scale. The utility of the approach is demonstrated with an application to an I58D mutant of the Pfl6 Cro protein that undergoes exchange between the native, folded state and a cold denatured, unfolded conformational ensemble that is populated at a level of 6% at 2.5°C. A wide distribution of amide temperature coefficients is measured for the unfolded state. The distribution is centered about -5.6 ppb/K, consistent with an absence of intra-molecular hydrogen bonds, on average. However, the large range of values (standard deviation of 2.1 ppb/K) strongly supports the notion that the unfolded state of the protein is not a true random coil polypeptide chain.

Type: Article
Title: Measuring 1HN temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy.
Location: Netherlands
DOI: 10.1007/s10858-011-9498-0
Keywords: Hydrogen Bonding, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, Proteins, Protons, Temperature
UCL classification: UCL > School of Life and Medical Sciences
UCL > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > School of Life and Medical Sciences > Faculty of Life Sciences > Biosciences (Division of) > Structural and Molecular Biology
URI: http://discovery.ucl.ac.uk/id/eprint/1308609
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