Approaches for the measurement of solvent exposure in proteins by 19F NMR Export

@article{citeulike:5402995, abstract = {Abstract\ \ Fluorine NMR is a useful tool to probe protein folding, conformation and local topology owing to the sensitivity of the chemical shift to the local electrostatic environment. As an example we make use of 19F NMR and 3-fluorotyrosine to evaluate the conformation and topology of the tyrosine residues (Tyr-99 and Tyr-138) within the EF-hand motif of the C-terminal domain of calmodulin (CaM) in both the calcium-loaded and calcium-free states. We critically compare approaches to assess topology and solvent exposure via solvent isotope shifts, 19F spin–lattice relaxation rates, 1H–19F nuclear Overhauser effects, and paramagnetic shifts and relaxation rates from dissolved oxygen. Both the solvent isotope shifts and paramagnetic shifts from dissolved oxygen sensitively reflect solvent exposed surface areas.}, author = {Kitevski-LeBlanc, Julianne and Evanics, Ferenc and Prosser, R.}, citeulike-article-id = {5402995}, citeulike-linkout-0 = {http://dx.doi.org/10.1007/s10858-009-9359-2}, citeulike-linkout-1 = {http://www.springerlink.com/content/x66571w80g65l764}, doi = {10.1007/s10858-009-9359-2}, journal = {Journal of Biomolecular NMR}, keywords = {19f, bulk-magnetization}, posted-at = {2009-09-30 22:27:30}, priority = {2}, title = {Approaches for the measurement of solvent exposure in proteins by 19F NMR}, url = {http://dx.doi.org/10.1007/s10858-009-9359-2} }

TY - JOUR ID - citeulike:5402995 L3 - citeulike-article-id:5402995 N2 - Abstract  Fluorine NMR is a useful tool to probe protein folding, conformation and local topology owing to the sensitivity of the chemical shift to the local electrostatic environment. As an example we make use of 19F NMR and 3-fluorotyrosine to evaluate the conformation and topology of the tyrosine residues (Tyr-99 and Tyr-138) within the EF-hand motif of the C-terminal domain of calmodulin (CaM) in both the calcium-loaded and calcium-free states. We critically compare approaches to assess topology and solvent exposure via solvent isotope shifts, 19F spin–lattice relaxation rates, 1H–19F nuclear Overhauser effects, and paramagnetic shifts and relaxation rates from dissolved oxygen. Both the solvent isotope shifts and paramagnetic shifts from dissolved oxygen sensitively reflect solvent exposed surface areas. JF - Journal of Biomolecular NMR TI - Approaches for the measurement of solvent exposure in proteins by 19F NMR KW - 19f KW - bulk-magnetization AU - Kitevski-LeBlanc, Julianne AU - Evanics, Ferenc AU - Prosser, R UR - http://dx.doi.org/10.1007/s10858-009-9359-2 ER -