NMR Determination of Residual Structure in a Urea-Denatured Protein, the 434-Repressor
- 11 September 1992
- journal article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 257 (5076), 1559-1563
- https://doi.org/10.1126/science.1523410
Abstract
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.Keywords
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