Interactions with Hydrophobic Clusters in the Urea‐Unfolded Membrane Protein OmpX
Journal article published in 2008 by
Sebastian Hiller 
,
Gerhard Wider,
Lukas L. Imbach ,
Kurt Wüthrich
,
Gerhard Wider,
Lukas L. Imbach ,
Kurt Wüthrich
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Abstract
A denatured membrane protein in 8 M urea was characterized. Two hydrophobic clusters, separated by 50 amino acids in the polypeptide chain, are shown to bind independently to detergent micelles (see picture). Long-range interactions between the two clusters are not observed. These observations provide new insights into protein folding mechanisms.