Folding of Ubiquitin: A Simple Model Describes the Strange Kinetics.

@article{citeulike:610249, abstract = {The ubiquitin mutant UbG folding experiments of Sabelko et al. (Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 6031-6036), in which "strange kinetics" were observed, are interpreted in terms of a simple kinetic model. A minimal set of states consisting of a semicompact globule, two off-pathway traps, and the native state are included; the fully unfolded state is not considered because folding to the semicompact globule is fast. Both the low- and the high-temperature experiments of Sabelko et al. are fitted by a system of kinetic equations determining the transitions between these states. It is possible that cold- and heat-denaturated states of UbG are the basis of the off-pathway traps. The fits of the kinetic model to the experimental results provides an estimate of the rate constants for the various reaction channels and show how their contributions vary with temperature. Introduction of an on-pathway intermediate instead of one of the off-pathway traps does not lead to agreement with the experiments.}, address = {Institute of Thermophysics, Siberian Branch of the Russian Academy of Sciences, Ac. Lavrent'ev av. 1, 630090 Novosibirsk, Russia, Laboratoire de Chimie Biophysique, ISIS, Universit\'{e} Louis Pasteur, Rue Blaise Pascal 4, 67000 Strasbourg, France, and Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138.}, author = {Chekmarev, Sergei F. and Krivov, Sergei V. and Karplus, Martin }, citeulike-article-id = {610249}, doi = {http://dx.doi.org/10.1021/jp056799o}, issn = {1520-6106}, journal = {J Phys Chem B Condens Matter Mater Surf Interfaces Biophys}, keywords = {folding}, month = {May}, number = {17}, pages = {8865--8869}, posted-at = {2006-05-01 17:59:19}, priority = {2}, title = {Folding of Ubiquitin: A Simple Model Describes the Strange Kinetics.}, url = {http://dx.doi.org/10.1021/jp056799o}, volume = {110}, year = {2006} }

TY - JOUR ID - citeulike:610249 L3 - citeulike-article-id:610249 TI - Folding of Ubiquitin: A Simple Model Describes the Strange Kinetics. JF - J Phys Chem B Condens Matter Mater Surf Interfaces Biophys VL - 110 IS - 17 SP - 8865 EP - 8869 AD - Institute of Thermophysics, Siberian Branch of the Russian Academy of Sciences, Ac. Lavrent'ev av. 1, 630090 Novosibirsk, Russia, Laboratoire de Chimie Biophysique, ISIS, Université Louis Pasteur, Rue Blaise Pascal 4, 67000 Strasbourg, France, and Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138. SN - 1520-6106 N2 - The ubiquitin mutant UbG folding experiments of Sabelko et al. (Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 6031-6036), in which "strange kinetics" were observed, are interpreted in terms of a simple kinetic model. A minimal set of states consisting of a semicompact globule, two off-pathway traps, and the native state are included; the fully unfolded state is not considered because folding to the semicompact globule is fast. Both the low- and the high-temperature experiments of Sabelko et al. are fitted by a system of kinetic equations determining the transitions between these states. It is possible that cold- and heat-denaturated states of UbG are the basis of the off-pathway traps. The fits of the kinetic model to the experimental results provides an estimate of the rate constants for the various reaction channels and show how their contributions vary with temperature. Introduction of an on-pathway intermediate instead of one of the off-pathway traps does not lead to agreement with the experiments. KW - folding AU - Chekmarev, Sergei AU - Krivov, Sergei AU - Karplus, Martin PY - 2006/05/04/ UR - http://dx.doi.org/10.1021/jp056799o ER -