Electric fields at the active site of an enzyme: direct comparison of experiment with theory. Export

@article{citeulike:1720986, abstract = {The electric fields produced in folded proteins influence nearly every aspect of protein function. We present a vibrational spectroscopy technique that measures changes in electric field at a specific site of a protein as shifts in frequency (Stark shifts) of a calibrated nitrile vibration. A nitrile-containing inhibitor is used to deliver a unique probe vibration to the active site of human aldose reductase, and the response of the nitrile stretch frequency is measured for a series of mutations in the enzyme active site. These shifts yield quantitative information on electric fields that can be directly compared with electrostatics calculations. We show that extensive molecular dynamics simulations and ensemble averaging are required to reproduce the observed changes in field.}, author = {Suydam, Ian T. and Snow, Christopher D. and Pande, Vijay S. and Boxer, Steven G.}, citeulike-article-id = {1720986}, citeulike-linkout-0 = {http://dx.doi.org/10.1126/science.1127159}, citeulike-linkout-1 = {http://www.sciencemag.org/cgi/content/abstract/313/5784/200}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/16840693}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=16840693}, day = {14}, doi = {10.1126/science.1127159}, issn = {1095-9203}, journal = {Science (New York, N.Y.)}, keywords = {electrostatics, pb}, month = {July}, number = {5784}, pages = {200--204}, posted-at = {2009-10-29 06:13:17}, priority = {2}, title = {Electric fields at the active site of an enzyme: direct comparison of experiment with theory.}, url = {http://dx.doi.org/10.1126/science.1127159}, volume = {313}, year = {2006} }

TY - JOUR ID - citeulike:1720986 L3 - citeulike-article-id:1720986 N2 - The electric fields produced in folded proteins influence nearly every aspect of protein function. We present a vibrational spectroscopy technique that measures changes in electric field at a specific site of a protein as shifts in frequency (Stark shifts) of a calibrated nitrile vibration. A nitrile-containing inhibitor is used to deliver a unique probe vibration to the active site of human aldose reductase, and the response of the nitrile stretch frequency is measured for a series of mutations in the enzyme active site. These shifts yield quantitative information on electric fields that can be directly compared with electrostatics calculations. We show that extensive molecular dynamics simulations and ensemble averaging are required to reproduce the observed changes in field. IS - 5784 JF - Science (New York, N.Y.) SN - 1095-9203 EP - 204 TI - Electric fields at the active site of an enzyme: direct comparison of experiment with theory. VL - 313 SP - 200 KW - electrostatics KW - pb AU - Suydam, Ian AU - Snow, Christopher AU - Pande, Vijay AU - Boxer, Steven PY - 2006/07/14/ UR - http://dx.doi.org/10.1126/science.1127159 ER -