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PROTEIN FOLDING: Making a Network of Hydrophobic Clusters
Robert L. Baldwin
The early events in protein folding are often difficult to track. A hydrophobic collapse, during which nonpolar residues are buried away from the polar solvent, has been proposed, but little is known about the role of this collapse in protein folding. In his Perspective, Baldwin discusses the report by Klein-Seetharaman et al., who shed some light on this issue. A network of hydrophobic clusters stabilizes at least one nonnative interaction in unfolded hen lysozyme. In conjunction with earlier studies, the results suggest that this network has a beneficial effect on the folding of the protein.
The author is in the Department of Biochemistry, Beckman Center, Stanford University School of Medicine, Stanford, CA, 94305-5307, USA.
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In Science Magazine
REPORTS
Judith Klein-Seetharaman, Maki Oikawa, Shaun B. Grimshaw, Julia Wirmer, Elke Duchardt, Tadashi Ueda, Taiji Imoto, Lorna J. Smith, Christopher M. Dobson, and Harald Schwalbe (1 March 2002) Science295 (5560), 1719.
[DOI: 10.1126/science.1067680] |Abstract »|Full Text »|PDF »|Supplemental Data »
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Detection of an Intermediate during Unfolding of Bacterial Cell Division Protein FtsZ: LOSS OF FUNCTIONAL PROPERTIES PRECEDES THE GLOBAL UNFOLDING OF FtsZ.
