Thu, 07 Aug 2008 22:04:31 BST CiteULike: cactus's Dyson http://www.citeulike.org/user/cactus/author/Dyson CiteULike.org en-gb Copyright © 2004-2008 citeulike.org http://www.citeulike.org/user/cactus/article/1011358 <i>Curr Opin Struct Biol, Vol. 12, No. 1. (February 2002), pp. 54-60.</i><br /><br />There are now numerous examples of proteins that are unstructured or only partially structured under physiological conditions and yet are nevertheless functional. Such proteins are especially prevalent in eukaryotes. In many cases, intrinsically disordered proteins adopt folded structures upon binding to their biological targets. Many new examples of coupled folding and binding events have been reported recently, providing new insights into mechanisms of molecular recognition. Coupling of folding and binding for unstructured proteins. HJ Dyson PE Wright Curr Opin Struct Biol, Vol. 12, No. 1. (February 2002), pp. 54-60. 2006-12-24T09:30:09-00:00 2002 Curr Opin Struct Biol 0959-440X 12 1 54 60 intrinsic_disorder protein ref-pc review http://www.citeulike.org/user/cactus/article/1323453 <i>Nature (23 May 2007)</i> Mechanism of coupled folding and binding of an intrinsically disordered protein Kenji Sugase Jane Dyson Peter Wright doi:10.1038/nature05858 Nature (23 May 2007) 2007-05-24T01:27:28-00:00 2007 Nature 0028-0836 Nature Publishing Group experiment intrinsic_disorder nmr protein http://www.citeulike.org/user/cactus/article/2764144 <i>Proceedings of the National Academy of Sciences, Vol. 105, No. 17. (29 April 2008), pp. 6278-6283.</i><br /><br />The primary driving force for protein folding is the sequestration of hydrophobic side chains from solvent water, but the means whereby the amino acid sequence directs the folding process to form the correct final folded state is not well understood. Measurements of NMR line broadening in spin-labeled samples of unfolded apomyoglobin at pH 2.3 have been used to derive a quantitative model for transient hydrophobic interactions between various sites in the polypeptide chain, as would occur during the initiation of protein folding. Local clusters of residues with high values for the parameter "average area buried upon folding" (AABUF) form foci not only for local contacts but for long-range interactions, the relative frequencies of which can be understood in terms of differences in the extent of reduction in chain configurational entropy that occurs upon formation of nonlocal contacts. These results complement the striking correlation previously observed between the kinetic folding process of apomyoglobin and the AABUF of its amino acid sequence [Nishimura C, Lietzow MA, Dyson HJ, Wright PE (2005) J Mol Biol 351:383-392]. For the acid-unfolded states of apomyoglobin, our approach identifies multiple distinct hydrophobic clusters of differing thermodynamic stability. The most structured of these clusters, although sparsely populated, have both native-like and nonnative character; the specificity of the transient long-range contacts observed in these states suggests that they play a key role in initiating chain collapse and folding. 10.1073/pnas.0710641105 Modeling transient collapsed states of an unfolded protein to provide insights into early folding events Daniel Felitsky Michael Lietzow Jane Dyson Peter Wright doi:10.1073/pnas.0710641105 Proceedings of the National Academy of Sciences, Vol. 105, No. 17. (29 April 2008), pp. 6278-6283. 2008-05-07T07:23:14-00:00 2008 Proceedings of the National Academy of Sciences 105 17 6278 6283 clip2 experiment folding nmr protein spin http://www.citeulike.org/user/cactus/article/1435321 <i>Nat Rev Mol Cell Biol, Vol. 6, No. 3. (March 2005), pp. 197-208.</i> INTRINSICALLY UNSTRUCTURED PROTEINS AND THEIR FUNCTIONS Jane Dyson Peter Wright doi:10.1038/nrm1589 Nat Rev Mol Cell Biol, Vol. 6, No. 3. (March 2005), pp. 197-208. 2007-07-05T07:53:02-00:00 2005 Nat Rev Mol Cell Biol 6 3 197 208 intrinsic_disorder protein review http://www.citeulike.org/user/cactus/article/108875 <i>Nature Reviews Molecular Cell Biology, Vol. 6, No. 3. (01 March 2005), pp. 197-208.</i> Intrinsically unstructured proteins and their functions Jane Dyson Peter Wright doi:10.1038/nrm1589 Nature Reviews Molecular Cell Biology, Vol. 6, No. 3. (01 March 2005), pp. 197-208. 2005-03-01T19:48:35-00:00 2005 Nature Reviews Molecular Cell Biology 1471-0072 6 3 197 208 Nature Publishing Group clip