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- W2009086370 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." @default.
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- W2009086370 date "2011-03-18" @default.
- W2009086370 modified "2023-10-09" @default.
- W2009086370 title "Measuring 1HN temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy" @default.
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- W2009086370 doi "https://doi.org/10.1007/s10858-011-9498-0" @default.
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