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Science 11 September 1992:
Vol. 257. no. 5076, pp. 1559 - 1563
DOI: 10.1126/science.1523410
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Articles

Science, Vol 257, Issue 5076, 1559-1563
Copyright © 1992 by American Association for the Advancement of Science

articles

NMR determination of residual structure in a urea-denatured protein, the 434-repressor

D Neri, M Billeter, G Wider, and K Wuthrich

Institut fur Molekularbiologie und Biophysik, ETH-Honggerberg, Zurich, Switzerland.

A nuclear magnetic resonance (NMR) structure determination is reported for the polypeptide chain of a globular protein in strongly denaturing solution. Nuclear Overhauser effect (NOE) measurements with a 7 molar urea solution of the amino-terminal 63-residue domain of the 434-repressor and distance geometry calculations showed that the polypeptide segment 54 to 59 forms a hydrophobic cluster containing the side chains of Val54, Val56, Trp58, and Leu59. This residual structure in the urea-unfolded protein is related to the corresponding region of the native, folded protein by simple rearrangements of the residues 58 to 60. Based on these observations a model for the early phase of refolding of the 434-repressor(1-63) is proposed.


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