Direct single-molecule observation of a protein living in two opposed native structures. Export

@article{citeulike:4792147, abstract = {Biological activity in proteins requires them to share the energy landscape for folding and global conformational motions, 2 key determinants of function. Although most structural studies to date have focused on fluctuations around a single structural basin, we directly observe the coexistence of 2 symmetrically opposed conformations for a mutant of the Rop-homodimer (Repressor of Primer) in single-molecule fluorescence resonance energy transfer (smFRET) measurements. We find that mild denaturing conditions can affect the sensitive balance between the conformations, generating an equilibrium ensemble consisting of 2 equally occupied structural basins. Despite the need for large-scale conformational rearrangement, both native structures are dynamically and reversibly adopted for the same paired molecules without separation of the constituent monomers. Such an ability of some proteins or protein complexes to switch between conformations by thermal fluctuations and/or minor environmental changes could be central to their ability to control biological function.}, author = {Gambin, Yann and Schug, Alexander and Lemke, Edward A. and Lavinder, Jason J. and Ferreon, Allan Chris C. and Magliery, Thomas J. and Onuchic, Jos\'{e} N. and Deniz, Ashok A.}, citeulike-article-id = {4792147}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.0904461106}, citeulike-linkout-1 = {http://www.pnas.org/content/0904461106v1//.abstract}, citeulike-linkout-2 = {http://www.pnas.org/content/0904461106v1//.full.pdf}, citeulike-linkout-3 = {http://view.ncbi.nlm.nih.gov/pubmed/19506258}, citeulike-linkout-4 = {http://www.hubmed.org/display.cgi?uids=19506258}, doi = {10.1073/pnas.0904461106}, issn = {1091-6490}, journal = {Proceedings of the National Academy of Sciences of the United States of America}, keywords = {fret, proteins, sms}, month = {June}, number = {25}, pages = {10153--10158}, posted-at = {2009-06-10 01:33:22}, priority = {2}, title = {Direct single-molecule observation of a protein living in two opposed native structures.}, url = {http://dx.doi.org/10.1073/pnas.0904461106}, volume = {106}, year = {2009} }

TY - JOUR ID - citeulike:4792147 L3 - citeulike-article-id:4792147 N2 - Biological activity in proteins requires them to share the energy landscape for folding and global conformational motions, 2 key determinants of function. Although most structural studies to date have focused on fluctuations around a single structural basin, we directly observe the coexistence of 2 symmetrically opposed conformations for a mutant of the Rop-homodimer (Repressor of Primer) in single-molecule fluorescence resonance energy transfer (smFRET) measurements. We find that mild denaturing conditions can affect the sensitive balance between the conformations, generating an equilibrium ensemble consisting of 2 equally occupied structural basins. Despite the need for large-scale conformational rearrangement, both native structures are dynamically and reversibly adopted for the same paired molecules without separation of the constituent monomers. Such an ability of some proteins or protein complexes to switch between conformations by thermal fluctuations and/or minor environmental changes could be central to their ability to control biological function. IS - 25 JF - Proceedings of the National Academy of Sciences of the United States of America SN - 1091-6490 EP - 10158 TI - Direct single-molecule observation of a protein living in two opposed native structures. VL - 106 SP - 10153 KW - fret KW - proteins KW - sms AU - Gambin, Yann AU - Schug, Alexander AU - Lemke, Edward AU - Lavinder, Jason AU - Ferreon, Allan Chris AU - Magliery, Thomas AU - Onuchic, José AU - Deniz, Ashok PY - 2009/06/23/ UR - http://dx.doi.org/10.1073/pnas.0904461106 ER -