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Protein dynamics in supercooled water: The search for slow motional modes

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Abstract

The impact of studying protein dynamics in supercooled water for identifying slow motional modes on the μs time scale is demonstrated. Backbone 15N spin relaxation parameters were measured at −13 °C for ubiquitin, which plays a central role for signaling proteolysis, cellular trafficking and kinase activation in eukaryotic organisms. A hitherto undetected motional mode involving Val 70 was found, which may well play an important role for ubiquitin recognition. The measurement of rotating frame 15N relaxation times as a function of the spin-lock field allowed determination of the correlation time of this motional mode, which would not have been feasible above 0 °C.

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Authors and Affiliations

  1. Department of Chemistry and Structural Biology, University at Buffalo, The State University of New York, Buffalo, NY, 14260, U.S.A

    Jeffrey L. Mills & Thomas Szyperski

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  1. Jeffrey L. Mills
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  2. Thomas Szyperski
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Correspondence to Thomas Szyperski.

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Mills, J.L., Szyperski, T. Protein dynamics in supercooled water: The search for slow motional modes. J Biomol NMR 23, 63–67 (2002). https://doi.org/10.1023/A:1015397305148

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