Rapid mixing methods for exploring the kinetics of protein folding Export

@article{citeulike:2890318, abstract = {Information on the time-dependence of molecular species is critical for elucidating reaction mechanisms in chemistry and biology. Rapid flow experiments involving turbulent mixing of two or more solutions continue to be the main source of kinetic information on protein folding and other biochemical processes, such as ligand binding and enzymatic reactions. Recent advances in mixer design and detection methods have opened a new window for exploring conformational changes in proteins on the microsecond time scale. These developments have been especially important for exploring early stages of protein folding.}, author = {Roder, Heinrich and Maki, Kosuke and Cheng, Hong and Ramachandra}, booktitle = {Investigating Protein Folding, Misfolding and Nonnative States: Experimental and Theoretical Methods}, citeulike-article-id = {2890318}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.ymeth.2004.03.003}, citeulike-linkout-1 = {http://www.sciencedirect.com/science/article/B6WN5-4CJVC6X-1/1/7934a5ffd58097914beca39a7d8da388}, doi = {10.1016/j.ymeth.2004.03.003}, journal = {Methods}, keywords = {biophysics, folding, kinetics}, month = {September}, number = {1}, pages = {15--27}, posted-at = {2008-06-13 03:05:42}, priority = {2}, title = {Rapid mixing methods for exploring the kinetics of protein folding}, url = {http://dx.doi.org/10.1016/j.ymeth.2004.03.003}, volume = {34}, year = {2004} }

TY - JOUR ID - citeulike:2890318 L3 - citeulike-article-id:2890318 N2 - Information on the time-dependence of molecular species is critical for elucidating reaction mechanisms in chemistry and biology. Rapid flow experiments involving turbulent mixing of two or more solutions continue to be the main source of kinetic information on protein folding and other biochemical processes, such as ligand binding and enzymatic reactions. Recent advances in mixer design and detection methods have opened a new window for exploring conformational changes in proteins on the microsecond time scale. These developments have been especially important for exploring early stages of protein folding. IS - 1 JF - Methods EP - 27 TI - Rapid mixing methods for exploring the kinetics of protein folding VL - 34 T2 - Investigating Protein Folding, Misfolding and Nonnative States: Experimental and Theoretical Methods SP - 15 KW - biophysics KW - folding KW - kinetics AU - Roder, Heinrich AU - Maki, Kosuke AU - Cheng, Hong AU - Ramachandra PY - 2004/09// UR - http://dx.doi.org/10.1016/j.ymeth.2004.03.003 ER -