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Nature Structural Biology  8, 659 - 660 (2001)
doi:10.1038/90349

Unfolded, yes, but random? Never!

Kevin W. Plaxco1 & Michael Gross2

1  Kevin W. Plaxco is at the Department of Chemistry and Biochemistry, University of California at Santa Barbara, Santa Barbara CA 93106, USA. kwp@chem.ucsb.edu

2  Michael Gross is at the Oxford Centre for Molecular Sciences, Central Chemistry Laboratory, Oxford OX1 3QH, UK. mgross@bioch.ox.ac.uk

NMR experiments with partially aligned protein molecules in strongly denaturing conditions suggest that the unfolded state is less chaotic than is widely believed. Hence protein folding is probably less paradoxical than Levinthal originally thought.

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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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