NMR and EPR studies of membrane transporters Export

@article{citeulike:6080168, abstract = {In order to fulfill their function, membrane transport proteins have to cycle through a number of conformational and/or energetic states. Thus, understanding the role of conformational dynamics seems to be the key for elucidation of the functional mechanism of these proteins. However, membrane proteins in general are often difficult to express heterologously and in sufficient amounts for structural studies. It is especially challenging to trap a stable energy minimum, e.g., for crystallographic analysis. Furthermore, crystallization is often only possible by subjecting the protein to conditions that do not resemble its native environment and crystals can only be snapshots of selected conformational states. Nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR) spectroscopy are complementary methods that offer unique possibilities for studying membrane proteins in their natural membrane environment and for investigating functional conformational changes, lipid interactions, substrate-lipid and substrate-protein interactions, oligomerization states and overall dynamics of membrane transporters. Here, we review recent progress in the field including studies from primary and secondary active transporters.}, author = {Hellmich, Ute A. and Glaubitz, Clemens}, citeulike-article-id = {6080168}, citeulike-linkout-0 = {http://www.reference-global.com/doi/abs/10.1515/BC.2009.084}, issn = {1437-4315}, journal = {Biological Chemistry}, keywords = {epr, membrane\_protein, nmr, transport\_proteins}, month = {August}, number = {8}, pages = {815--834}, posted-at = {2009-11-06 08:36:55}, priority = {2}, title = {NMR and EPR studies of membrane transporters}, url = {http://www.reference-global.com/doi/abs/10.1515/BC.2009.084}, volume = {390}, year = {2009} }

TY - JOUR ID - citeulike:6080168 L3 - citeulike-article-id:6080168 N2 - In order to fulfill their function, membrane transport proteins have to cycle through a number of conformational and/or energetic states. Thus, understanding the role of conformational dynamics seems to be the key for elucidation of the functional mechanism of these proteins. However, membrane proteins in general are often difficult to express heterologously and in sufficient amounts for structural studies. It is especially challenging to trap a stable energy minimum, e.g., for crystallographic analysis. Furthermore, crystallization is often only possible by subjecting the protein to conditions that do not resemble its native environment and crystals can only be snapshots of selected conformational states. Nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR) spectroscopy are complementary methods that offer unique possibilities for studying membrane proteins in their natural membrane environment and for investigating functional conformational changes, lipid interactions, substrate-lipid and substrate-protein interactions, oligomerization states and overall dynamics of membrane transporters. Here, we review recent progress in the field including studies from primary and secondary active transporters. IS - 8 JF - Biological Chemistry SN - 1437-4315 EP - 834 TI - NMR and EPR studies of membrane transporters VL - 390 SP - 815 KW - epr KW - membrane_protein KW - nmr KW - transport_proteins AU - Hellmich, Ute AU - Glaubitz, Clemens PY - 2009/08// UR - http://www.reference-global.com/doi/abs/10.1515/BC.2009.084 ER -