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International
Tables for Crystallography Volume F Crystallography of biological macromolecules Edited by M. G. Rossmann and E. Arnold © International Union of Crystallography 2006 |
International Tables for Crystallography (2006). Vol. F. ch. 19.3, p. 437
Section 19.3.3.4.3. Protein-folding studies
a
SSRL/SLAC & Department of Chemistry, Stanford University, PO Box 4349, MS69, Stanford, California 94309-0210, USA, and bDepartment of Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, California 92037, USA |
There have been a number of solution X-ray scattering studies on protein folding in recent years, in which proteins of low molecular weight had to be investigated under low electron-density contrast due to the presence of denaturing agents, such as urea, at high concentration. Solution X-ray scattering complements other structural techniques used in protein-folding studies, as this is the only technique available for learning how compact a protein is in solution. A Kratky plot of solution scattering data serves as a quick means of determining whether a protein is folded or unfolded. Recently, the singular value decomposition method was applied to this class of problems and revealed a folding intermediate of lysozyme (Chen et al., 1996![[link]](/graphics/greenarr.gif)
). This study has recently been expanded to a time-resolved study, which revealed a compact folding intermediate that has not yet formed a hydrophobic core (Chen et al., 1998). Similar studies are being carried out on other protein systems. Arai et al. (1998) reported that β-lactoglobulin undergoes a similar folding pattern while it forms a folding intermediate with a hydrophobic core within 100 ms. Uversky et al. (1998) reported association-induced folding of globular proteins. Pollack et al. (1999) developed a micro-machined mixer to study folding of cytochrome c in the sub-millisecond regime.
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