A pre-existing hydrophobic collapse in the unfolded state of an ultrafast folding protein

K. Hun Mok (), Lars T. Kuhn, Martin Goez, Iain J. Day, Jasper C. Lin, Niels H. Andersen and P. J. Hore ()
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K. Hun Mok: University of Oxford, Physical & Theoretical Chemistry Laboratory, South Parks Road, Oxford OX1 3QZ, UK
Lars T. Kuhn: University of Oxford, Physical & Theoretical Chemistry Laboratory, South Parks Road, Oxford OX1 3QZ, UK
Martin Goez: Fachbereich Chemie, Martin-Luther-Universität Halle-Wittenberg, Kurt-Mothes-Strasse 2, D-06120 Halle/Saale, Germany
Iain J. Day: University of Massachusetts Medical School, 364 Plantation Street, Worcester, Massachusetts 01605, USA
Jasper C. Lin: University of Washington, Seattle, Washington 98195, USA
Niels H. Andersen: University of Washington, Seattle, Washington 98195, USA
P. J. Hore: University of Oxford, Physical & Theoretical Chemistry Laboratory, South Parks Road, Oxford OX1 3QZ, UK

Nature, 2007, vol. 447, issue 7140, 106-109

Abstract: A nuclear magnetic resonance technique is developed that allows early atomic interactions to be read out later, in the more homogeneous folded state. When this is applied to an ultrafast folding designer protein, it discovers an early hydrophobic core that had been overlooked by computational models.

Date: 2007
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DOI: 10.1038/nature05728

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