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2
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5644258235
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+ channel in a lipid bilayer
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+ channel KvAP in depolarized membranes. The work shows that S4 is located near the interface and is highly dynamic.
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+ channel KvAP in depolarized membranes. The work shows that S4 is located near the interface and is highly dynamic.
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Cuello, L.G.1
Cortes, D.M.2
Perozo, E.3
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3
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0037452539
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Substrate-induced conformational changes of the perplasmic N-terminus of an outer-membrane transporter by site-directed spin labeling
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Fanucci G.E., Coggshall K.A., Cadieux N., Kim M., Kadner R.J., and Cafiso D.S. Substrate-induced conformational changes of the perplasmic N-terminus of an outer-membrane transporter by site-directed spin labeling. Biochemistry 42 (2003) 1391-1400
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Fanucci, G.E.1
Coggshall, K.A.2
Cadieux, N.3
Kim, M.4
Kadner, R.J.5
Cafiso, D.S.6
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4
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25144470549
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Mapping of the docking of SecA onto the chaperone SecB by site-directed spin labeling: insight into the mechanism of ligand transfer during protein export
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EPR spectroscopy has been used to investigate the interactions between SecB and SecA, the chaperone and ATPase that enable capture of precursor polypeptides for insertion into the translocon of the protein secretory system of Gram-negative bacteria. In this study, 41 spin-labeled derivatives of SecB were produced, all of which were found to fold correctly and to bind SecA. From the changes in the EPR lineshapes that occur upon interaction, SecA was found to interact across the long dimer interface of SecB.
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Crane J.M., Mao C., Lilly A.A., Smith V.F., Suo Y., Hubbell W.L., and Randall L.L. Mapping of the docking of SecA onto the chaperone SecB by site-directed spin labeling: insight into the mechanism of ligand transfer during protein export. J Mol Biol 353 (2005) 295-307. EPR spectroscopy has been used to investigate the interactions between SecB and SecA, the chaperone and ATPase that enable capture of precursor polypeptides for insertion into the translocon of the protein secretory system of Gram-negative bacteria. In this study, 41 spin-labeled derivatives of SecB were produced, all of which were found to fold correctly and to bind SecA. From the changes in the EPR lineshapes that occur upon interaction, SecA was found to interact across the long dimer interface of SecB.
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J Mol Biol
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Crane, J.M.1
Mao, C.2
Lilly, A.A.3
Smith, V.F.4
Suo, Y.5
Hubbell, W.L.6
Randall, L.L.7
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5
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0028346566
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A collision gradient method to determine the immersion depth of nitroxides in lipid bilayers: application to spin-labeled mutants of bacteriorhodopsin
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Altenbach C., Greenhalgh D.A., Khorana H.G., and Hubbell W.L. A collision gradient method to determine the immersion depth of nitroxides in lipid bilayers: application to spin-labeled mutants of bacteriorhodopsin. Proc Natl Acad Sci USA 91 (1994) 1667-1671
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Altenbach, C.1
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18644362391
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Structural basis of energy transduction in the transport cycle of MsbA
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The authors used SDSL to investigate the structures and conformational changes that couple ATP hydrolysis to substrate transport in the multidrug transporter MsbA. The authors find differences in packing and water penetration compared with the crystal structure of this protein.
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Dong J., Yang G., and McHaourab H.S. Structural basis of energy transduction in the transport cycle of MsbA. Science 308 (2005) 1023-1028. The authors used SDSL to investigate the structures and conformational changes that couple ATP hydrolysis to substrate transport in the multidrug transporter MsbA. The authors find differences in packing and water penetration compared with the crystal structure of this protein.
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Science
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Dong, J.1
Yang, G.2
McHaourab, H.S.3
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7
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15244339850
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Site-directed spin labeling reveals a conformational switch in the phosphorylation domain of smooth muscle myosin
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SDSL was used to examine the effect of phosphorylation on the regulatory light chain of smooth muscle myosin. The authors provide evidence that the N-terminal domain undergoes an increase in helical order when phosphorylated, but also has increased dynamics and accessibility. The authors propose a model for the role of this disorder-to-order transition in activating smooth muscle.
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Nelson W.D., Blakely S.E., Nesmelov Y.E., and Thomas D.D. Site-directed spin labeling reveals a conformational switch in the phosphorylation domain of smooth muscle myosin. Proc Natl Acad Sci USA 102 (2005) 4000-4005. SDSL was used to examine the effect of phosphorylation on the regulatory light chain of smooth muscle myosin. The authors provide evidence that the N-terminal domain undergoes an increase in helical order when phosphorylated, but also has increased dynamics and accessibility. The authors propose a model for the role of this disorder-to-order transition in activating smooth muscle.
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(2005)
Proc Natl Acad Sci USA
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, pp. 4000-4005
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Nelson, W.D.1
Blakely, S.E.2
Nesmelov, Y.E.3
Thomas, D.D.4
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8
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0029115328
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Determination of the distance between two spin labels attached to a macromolecule
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Rabenstein M.D., and Shin Y.K. Determination of the distance between two spin labels attached to a macromolecule. Proc Natl Acad Sci USA 92 (1995) 8239-8243
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Proc Natl Acad Sci USA
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Rabenstein, M.D.1
Shin, Y.K.2
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0035951101
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Estimation of inter-residue distances in spin labeled proteins at physiological temperatures: experimental strategies and practical limitations
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Altenbach C., Oh K.J., Trabanino R.J., Hideg K., and Hubbell W.L. Estimation of inter-residue distances in spin labeled proteins at physiological temperatures: experimental strategies and practical limitations. Biochemistry 40 (2001) 15471-15482
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Biochemistry
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Altenbach, C.1
Oh, K.J.2
Trabanino, R.J.3
Hideg, K.4
Hubbell, W.L.5
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11
-
-
2942527068
-
Mapping backbone dynamics in solution with site-directed spin labeling: GCN4-58 bZip free and bound to DNA
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In this work, the authors examine the DNA-binding region of GCN4 and demonstrate that the mobility of the nitroxide sidechain mirrors backbone motion along the DNA-binding helix.
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Columbus L., and Hubbell W.L. Mapping backbone dynamics in solution with site-directed spin labeling: GCN4-58 bZip free and bound to DNA. Biochemistry 43 (2004) 7273-7287. In this work, the authors examine the DNA-binding region of GCN4 and demonstrate that the mobility of the nitroxide sidechain mirrors backbone motion along the DNA-binding helix.
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(2004)
Biochemistry
, vol.43
, pp. 7273-7287
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Columbus, L.1
Hubbell, W.L.2
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12
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-
0035799354
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Molecular motion of spin labeled side chains in alpha-helices: analysis by variation of side chain structure
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Columbus L., Kalai T., Jeko J., Hideg K., and Hubbell W.L. Molecular motion of spin labeled side chains in alpha-helices: analysis by variation of side chain structure. Biochemistry 40 (2001) 3828-3846
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Biochemistry
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, pp. 3828-3846
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Columbus, L.1
Kalai, T.2
Jeko, J.3
Hideg, K.4
Hubbell, W.L.5
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13
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1542428959
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Motion of spin label side chains in cellular retinol-binding protein: correlation with structure and nearest-neighbor interactions in an antiparallel beta-sheet
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Lietzow M.A., and Hubbell W.L. Motion of spin label side chains in cellular retinol-binding protein: correlation with structure and nearest-neighbor interactions in an antiparallel beta-sheet. Biochemistry 43 (2004) 3137-3151
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Lietzow, M.A.1
Hubbell, W.L.2
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0037093869
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Protein structure determination using long-distance constraints from double-quantum coherence ESR: study of T4 lysozyme
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Borbat P.P., Mchaourab H., and Freed J.H. Protein structure determination using long-distance constraints from double-quantum coherence ESR: study of T4 lysozyme. J Am Chem Soc 124 (2002) 5304-5314
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Borbat, P.P.1
Mchaourab, H.2
Freed, J.H.3
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15
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33646127590
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Dipolar coupling between nitroxide spin labels: the development and application of a tether-in-a-cone model
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This work provides a discussion of how distance distributions may be affected by the orientation of labels and their motion.
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Hustedt E.J., Stein R.A., Sethaphong L., Brandon S., Zhou Z., and Desensi S.C. Dipolar coupling between nitroxide spin labels: the development and application of a tether-in-a-cone model. Biophys J 90 (2006) 340-356. This work provides a discussion of how distance distributions may be affected by the orientation of labels and their motion.
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Biophys J
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Hustedt, E.J.1
Stein, R.A.2
Sethaphong, L.3
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Zhou, Z.5
Desensi, S.C.6
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Distance measurements in the nanometer range by pulse EPR
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Jeschke G. Distance measurements in the nanometer range by pulse EPR. ChemPhysChem 3 (2002) 927-932
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Jeschke, G.1
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21644446664
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Explicit treatment of spin labels in modeling of distance constraints from dipolar EPR and DEER
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Sale K., Song L., Liu Y.S., Perozo E., and Fajer P. Explicit treatment of spin labels in modeling of distance constraints from dipolar EPR and DEER. J Am Chem Soc 127 (2005) 9334-9335
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Sale, K.1
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Fajer, P.5
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0041154173
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Motion of spin-labeled side chains in T4 lysozyme: effect of side chain structure
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McHaourab H.S., Kalai T., Hideg K., and Hubbell W.L. Motion of spin-labeled side chains in T4 lysozyme: effect of side chain structure. Biochemistry 38 (1999) 2947-2955
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Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics
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McHaourab H.S., Lietzow M.A., Hideg K., and Hubbell W.L. Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics. Biochemistry 35 (1996) 7692-7704
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McHaourab, H.S.1
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Hubbell, W.L.4
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20
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0000326938
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Nonlinear-least-squares analysis of slow-motion EPR spectra in one and two dimensions using a modified Levenberg-Marquardt algorithm
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Budil D.E., Lee S., Saxena S., and Freed J.H. Nonlinear-least-squares analysis of slow-motion EPR spectra in one and two dimensions using a modified Levenberg-Marquardt algorithm. J Magn Reson A 120 (1996) 155-189
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Budil, D.E.1
Lee, S.2
Saxena, S.3
Freed, J.H.4
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21
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33646942808
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Visual arrestin binding to microtubules involves a distinct conformational change
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Hanson S.M., Francis D.J., Vishnivetskiy S.A., Klug C.S., and Gurevich V.V. Visual arrestin binding to microtubules involves a distinct conformational change. J Biol Chem 281 (2006) 9765-9772
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Hanson, S.M.1
Francis, D.J.2
Vishnivetskiy, S.A.3
Klug, C.S.4
Gurevich, V.V.5
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22
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27644581213
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Combining high-field EPR with site-directed spin labeling reveals unique information on proteins in action
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Mobius K., Savitsky A., Wegener C., Plato M., Fuchs M., Schnegg A., Dubinskii A.A., Grishin Y.A., Grigor'ev I.A., Kuhn M., et al. Combining high-field EPR with site-directed spin labeling reveals unique information on proteins in action. Magn Reson Chem 43 (2005) S4-S19
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Magn Reson Chem
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Mobius, K.1
Savitsky, A.2
Wegener, C.3
Plato, M.4
Fuchs, M.5
Schnegg, A.6
Dubinskii, A.A.7
Grishin, Y.A.8
Grigor'ev, I.A.9
Kuhn, M.10
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23
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33645505709
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Calculating slow-motional electron paramagnetic resonance spectra from molecular dynamics using a diffusion operator approach
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Computing EPR spectra from MD trajectories is a challenging task, in part because of the relatively long timescales sensed by spin labels. In this work, the authors show how MD trajectories may be used to set diffusion and geometric parameters in a diffusion-operator-based formalism that is widely used to calculate EPR spectra.
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Budil D.E., Sale K.L., Khairy K.A., and Fajer P.G. Calculating slow-motional electron paramagnetic resonance spectra from molecular dynamics using a diffusion operator approach. J Phys Chem A Mol Spectrosc Kinet Environ Gen Theory 110 (2006) 3703-3713. Computing EPR spectra from MD trajectories is a challenging task, in part because of the relatively long timescales sensed by spin labels. In this work, the authors show how MD trajectories may be used to set diffusion and geometric parameters in a diffusion-operator-based formalism that is widely used to calculate EPR spectra.
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(2006)
J Phys Chem A Mol Spectrosc Kinet Environ Gen Theory
, vol.110
, pp. 3703-3713
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Budil, D.E.1
Sale, K.L.2
Khairy, K.A.3
Fajer, P.G.4
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24
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33644838909
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Influence of the disulfide bond configuration on the dynamics of the spin label attached to cytochrome c
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Murzyn K., Rog T., Blicharski W., Dutka M., Pyka J., Szytula S., and Froncisz W. Influence of the disulfide bond configuration on the dynamics of the spin label attached to cytochrome c. Proteins 62 (2006) 1088-1100
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Proteins
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Murzyn, K.1
Rog, T.2
Blicharski, W.3
Dutka, M.4
Pyka, J.5
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Froncisz, W.7
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25
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27944506894
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Solution structure of the cytoplasmic domain of erythrocyte membrane band 3 determined by site-directed spin labeling
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This very nice study combines a series of CW and pulse EPR techniques to examine the structure of the cytoplasmic domain of the erythrocyte anion exchange protein. The data show that the crystal structure is valid in solution and the authors identify regions of disordered structure.
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Zhou Z., DeSensi S.C., Stein R.A., Brandon S., Dixit M., McArdle E.J., Warren E.M., Kroh H.K., Song L., Cobb C.E., et al. Solution structure of the cytoplasmic domain of erythrocyte membrane band 3 determined by site-directed spin labeling. Biochemistry 44 (2005) 15115-15128. This very nice study combines a series of CW and pulse EPR techniques to examine the structure of the cytoplasmic domain of the erythrocyte anion exchange protein. The data show that the crystal structure is valid in solution and the authors identify regions of disordered structure.
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(2005)
Biochemistry
, vol.44
, pp. 15115-15128
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Zhou, Z.1
DeSensi, S.C.2
Stein, R.A.3
Brandon, S.4
Dixit, M.5
McArdle, E.J.6
Warren, E.M.7
Kroh, H.K.8
Song, L.9
Cobb, C.E.10
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26
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33645506641
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Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin
-
Spin labels were attached to 28 sites in visual arrestin and EPR was used to characterize the complex with rhodopsin in its phosphorylated state. The authors describe unique complexes in both the dark and light-activated states of rhodopsin, and identify key recognition sites when arrestin interacts with activated rhodopsin.
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Hanson S.M., Francis D.J., Vishnivetskiy S.A., Kolobova E.A., Hubbell W.L., Klug C.S., and Gurevich V.V. Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin. Proc Natl Acad Sci USA 103 (2006) 4900-4905. Spin labels were attached to 28 sites in visual arrestin and EPR was used to characterize the complex with rhodopsin in its phosphorylated state. The authors describe unique complexes in both the dark and light-activated states of rhodopsin, and identify key recognition sites when arrestin interacts with activated rhodopsin.
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(2006)
Proc Natl Acad Sci USA
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Hanson, S.M.1
Francis, D.J.2
Vishnivetskiy, S.A.3
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Hubbell, W.L.5
Klug, C.S.6
Gurevich, V.V.7
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27
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23244454211
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+ antiporter of E coli
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This interesting study demonstrates the potential of long-range distance measurements, such as those obtained from DEER, to examine the oligomerization state of membrane proteins.
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+ antiporter of E coli. Biophys J 89 (2005) 1328-1338. This interesting study demonstrates the potential of long-range distance measurements, such as those obtained from DEER, to examine the oligomerization state of membrane proteins.
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Electron electron double-resonance in electron-spin echo-model biradical systems and the sensitized photolysis of decalin
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Measurement of large distances in biomolecules using double-quantum filtered refocused electron spin-echoes
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A variant of the six-pulse DQC experiment is described that suppresses the effects of nuclear spin diffusion and enables accurate distance measurements to about 70 Å.
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Borbat P.P., Davis J.H., Butcher S.E., and Freed J.H. Measurement of large distances in biomolecules using double-quantum filtered refocused electron spin-echoes. J Am Chem Soc 126 (2004) 7746-7747. A variant of the six-pulse DQC experiment is described that suppresses the effects of nuclear spin diffusion and enables accurate distance measurements to about 70 Å.
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33645947031
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Isotope selection in distance measurements between nitroxides
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15N nitroxides are shown to be valuable for calculating distances when multiple spin pairs are present in macromolecules or macromolecular complexes.
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15N nitroxides are shown to be valuable for calculating distances when multiple spin pairs are present in macromolecules or macromolecular complexes.
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Piton N., Schiemann O., Mu Y., Stock G., Prisner T., and Engels J.W. Synthesis of spin-labeled RNAs for long range distance measurements by PELDOR. Nucleosides Nucleotides Nucleic Acids 24 (2005) 771-775
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Suppression of electron spin-echo envelope modulation peaks in double quantum coherence electron spin resonance
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This article presents a nice description of the instrumentation requirements for pulse experiments. It also describes a procedure to suppress unwanted peaks in DQC electron spin resonance (ESR) spectra that arise from electron-nuclear dipolar coupling. The implementation of this experiment on commercial instrumentation at X-band is discussed.
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Bonora M., Becker J., and Saxena S. Suppression of electron spin-echo envelope modulation peaks in double quantum coherence electron spin resonance. J Magn Reson 170 (2004) 278-283. This article presents a nice description of the instrumentation requirements for pulse experiments. It also describes a procedure to suppress unwanted peaks in DQC electron spin resonance (ESR) spectra that arise from electron-nuclear dipolar coupling. The implementation of this experiment on commercial instrumentation at X-band is discussed.
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J Magn Reson
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Bonora, M.1
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Saxena, S.3
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Comparing continuous wave progressive saturation EPR and time domain saturation recovery EPR over the entire motional range of nitroxide spin labels
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Nielsen R.D., Canaan S., Gladden J.A., Gelb M.H., Mailer C., and Robinson B.H. Comparing continuous wave progressive saturation EPR and time domain saturation recovery EPR over the entire motional range of nitroxide spin labels. J Magn Reson 169 (2004) 129-163
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J Magn Reson
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Nielsen, R.D.1
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The authors show that power saturation techniques provide an accurate measure of the exchange rate between a protein-associated nitroxide and a paramagnetic reagent in solution. In addition, accessibility factors of the nitroxides are shown to correlate with structure-based accessibilities.
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Altenbach C., Froncisz W., Hemker R., McHaourab H., and Hubbell W.L. Accessibility of nitroxide side chains: absolute Heisenberg exchange rates from power saturation EPR. Biophys J 89 (2005) 2103-2112. The authors show that power saturation techniques provide an accurate measure of the exchange rate between a protein-associated nitroxide and a paramagnetic reagent in solution. In addition, accessibility factors of the nitroxides are shown to correlate with structure-based accessibilities.
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17844402249
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Multiquantum EPR spectroscopy of spin-labeled arrestin K267C at 35 GHz
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2. Using a loop-gap resonator with a 30 nL sample volume, spectra were obtained using 1 pmol of protein.
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2. Using a loop-gap resonator with a 30 nL sample volume, spectra were obtained using 1 pmol of protein.
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Ball, A.1
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Identification of protein side chains near the membrane-aqueous interface: a site-directed spin labeling study of KcsA
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Gross A., and Hubbell W.L. Identification of protein side chains near the membrane-aqueous interface: a site-directed spin labeling study of KcsA. Biochemistry 41 (2002) 1123-1128
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Gross, A.1
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42
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Atomic models by cryo-EM and site-directed spin labeling: application to the N-terminal region of Hsp16.5
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This work describes the novel application of information from SDSL to refine a segment of Hsp16.5 that is not resolved by electron diffraction.
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Koteiche H.A., Chiu S., Majdoch R.L., Stewart P.L., and McHaourab H.S. Atomic models by cryo-EM and site-directed spin labeling: application to the N-terminal region of Hsp16.5. Structure 13 (2005) 1165-1171. This work describes the novel application of information from SDSL to refine a segment of Hsp16.5 that is not resolved by electron diffraction.
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Structure
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Koteiche, H.A.1
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43
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24644511078
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Membrane structures of the hemifusion-inducing fusion peptide mutant G1S and the fusion-blocking mutant G1V of influenza virus hemagglutinin suggest a mechanism for pore opening in membrane fusion
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This work combines structural data from NMR and depth data from SDSL to determine the structures and positions of fusion peptides, and selected mutants, within the lipid bilayer. It indicates that the shape and position assumed by these peptides is important for their fusion activity.
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Li Y., Han X., Lai A.L., Bushweller J.H., Cafiso D.S., and Tamm L.K. Membrane structures of the hemifusion-inducing fusion peptide mutant G1S and the fusion-blocking mutant G1V of influenza virus hemagglutinin suggest a mechanism for pore opening in membrane fusion. J Virol 79 (2005) 12065-12076. This work combines structural data from NMR and depth data from SDSL to determine the structures and positions of fusion peptides, and selected mutants, within the lipid bilayer. It indicates that the shape and position assumed by these peptides is important for their fusion activity.
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(2005)
J Virol
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Li, Y.1
Han, X.2
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Bushweller, J.H.4
Cafiso, D.S.5
Tamm, L.K.6
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44
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33747453911
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Position of synaptotagmin I at the membrane interface: cooperative interactions of tandem C2 domains
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2+-dependent exocytosis. When present together, the two domains have a similar orientation to that of each isolated domain, but they penetrate more deeply into the bilayer than either domain alone.
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2+-dependent exocytosis. When present together, the two domains have a similar orientation to that of each isolated domain, but they penetrate more deeply into the bilayer than either domain alone.
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(2006)
Biochemistry
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, pp. 9668-9674
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Herrick, D.Z.1
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45
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11844254393
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Rufener E., Frazier A.A., Wieser C.M., Hinderliter A., and Cafiso D.S. Membrane-bound orientation and position of the synaptotagmin C2B domain determined by site-directed spin labeling. Biochemistry 44 (2005) 18-28
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Rufener, E.1
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Kohout S.C., Corbalan-Garcia S., Gomez-Fernandez J.C., and Falke J.J. C2 domain of protein kinase C alpha: elucidation of the membrane docking surface by site-directed fluorescence and spin labeling. Biochemistry 42 (2003) 1254-1265
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Malmberg N.J., Van Buskirk D.R., and Falke J.J. Membrane-docking loops of the cPLA2 C2 domain: detailed structural analysis of the protein-membrane interface via site-directed spin-labeling. Biochemistry 42 (2003) 13227-13240
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31044455230
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A novel calcium-independent peripheral membrane-bound form of annexin B12
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2+-independent binding of annexin B12 to bilayers occurs, evidence of the pH-dependent insertion of a helical region is presented. The authors suggest that the surface-associated form may be a kinetic intermediate on the path to the transmembrane form of the protein.
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2+-independent binding of annexin B12 to bilayers occurs, evidence of the pH-dependent insertion of a helical region is presented. The authors suggest that the surface-associated form may be a kinetic intermediate on the path to the transmembrane form of the protein.
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Biochemistry
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Hegde, B.G.1
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49
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A helical hairpin region of soluble annexin B12 refolds and forms a continuous transmembrane helix at mildly acidic pH
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Kim Y.E., Isas J.M., Haigler H.T., and Langen R. A helical hairpin region of soluble annexin B12 refolds and forms a continuous transmembrane helix at mildly acidic pH. J Biol Chem 280 (2005) 32398-32404
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Kim, Y.E.1
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50
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Bhargava K., and Feix J.B. Membrane binding, structure, and localization of cecropin-mellitin hybrid peptides: a site-directed spin-labeling study. Biophys J 86 (2004) 329-336
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Bhargava, K.1
Feix, J.B.2
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51
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33645210449
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Deimination of membrane-bound myelin basic protein in multiple sclerosis exposes an immunodominant epitope
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This work examines two forms of the immunodominant epitope of myelin basic protein. It shows that they assume different configurations when bound to membrane interfaces and have different exposure to proteases. The work suggests a mechanism for the loss of myelin stability.
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Musse A.A., Boggs J.M., and Harauz G. Deimination of membrane-bound myelin basic protein in multiple sclerosis exposes an immunodominant epitope. Proc Natl Acad Sci USA 103 (2006) 4422-4427. This work examines two forms of the immunodominant epitope of myelin basic protein. It shows that they assume different configurations when bound to membrane interfaces and have different exposure to proteases. The work suggests a mechanism for the loss of myelin stability.
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Proc Natl Acad Sci USA
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Musse, A.A.1
Boggs, J.M.2
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53
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16844381206
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Characterization of the Walker A motif of MsbA using site-directed spin labeling electron paramagnetic resonance spectroscopy
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Spin labels were incorporated into the region of MsbA that directly binds ATP, but is not resolved in the crystal structure. The authors demonstrate that this segment is helical, consistent with the structures of other members of this ABC transporter protein family.
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Buchaklian A.H., and Klug C.S. Characterization of the Walker A motif of MsbA using site-directed spin labeling electron paramagnetic resonance spectroscopy. Biochemistry 44 (2005) 5503-5509. Spin labels were incorporated into the region of MsbA that directly binds ATP, but is not resolved in the crystal structure. The authors demonstrate that this segment is helical, consistent with the structures of other members of this ABC transporter protein family.
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Biochemistry
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Buchaklian, A.H.1
Klug, C.S.2
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54
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Membrane mimetic environments alter the conformation of the outer membrane protein BtuB
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Fanucci G.E., Lee J.Y., and Cafiso D.S. Membrane mimetic environments alter the conformation of the outer membrane protein BtuB. J Am Chem Soc 125 (2003) 13932-13933
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Fanucci, G.E.1
Lee, J.Y.2
Cafiso, D.S.3
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55
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Spectroscopic evidence that osmolytes used in crystallization buffers inhibit a conformation change in a membrane protein
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Fanucci G.E., Lee J.Y., and Cafiso D.S. Spectroscopic evidence that osmolytes used in crystallization buffers inhibit a conformation change in a membrane protein. Biochemistry 42 (2003) 13106-13112
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Fanucci, G.E.1
Lee, J.Y.2
Cafiso, D.S.3
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56
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33646202285
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Solutes modify a conformational transition in a membrane transport protein
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This work shows that a conformational change seen by EPR may be modulated by solution osmolality and that the sensitivity to osmolality is consistent with the structural change observed. This observation provides a likely explanation for the absence of this transition in the protein crystal structure.
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Kim M., Xu Q., Fanucci G.E., and Cafiso D.S. Solutes modify a conformational transition in a membrane transport protein. Biophys J 90 (2006) 2922-2929. This work shows that a conformational change seen by EPR may be modulated by solution osmolality and that the sensitivity to osmolality is consistent with the structural change observed. This observation provides a likely explanation for the absence of this transition in the protein crystal structure.
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Biophys J
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Kim, M.1
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Cafiso, D.S.4
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57
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4344674667
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Structural origins of constitutive activation in rhodopsin: role of the K296/E113 salt bridge
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This interesting paper demonstrates the connection between mutations that lead to the constitutive activation of rhodopsin and the structural change that activates transducin.
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Kim J.M., Altenbach C., Kono M., Oprian D.D., Hubbell W.L., and Khorana H.G. Structural origins of constitutive activation in rhodopsin: role of the K296/E113 salt bridge. Proc Natl Acad Sci USA 101 (2004) 12508-12513. This interesting paper demonstrates the connection between mutations that lead to the constitutive activation of rhodopsin and the structural change that activates transducin.
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Proc Natl Acad Sci USA
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Kim, J.M.1
Altenbach, C.2
Kono, M.3
Oprian, D.D.4
Hubbell, W.L.5
Khorana, H.G.6
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58
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Hemifusion in SNARE-mediated membrane fusion
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Xu Y., Zhang F., Su Z., McNew J.A., and Shin Y.K. Hemifusion in SNARE-mediated membrane fusion. Nat Struct Mol Biol 12 (2005) 417-422
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Xu, Y.1
Zhang, F.2
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McNew, J.A.4
Shin, Y.K.5
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59
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33645543156
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Transmembrane organization of yeast syntaxin-analogue Sso1p
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This work examines the topology of the transmembrane domain of a yeast T-SNARE involved in membrane trafficking. It also indicates the existence of an equilibrium between monomers and oligomers of this domain. In addition, the authors nicely illustrate the dependence of the hyperfine splitting on membrane depth.
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Zhang Y., and Shin Y.K. Transmembrane organization of yeast syntaxin-analogue Sso1p. Biochemistry 45 (2006) 4173-4181. This work examines the topology of the transmembrane domain of a yeast T-SNARE involved in membrane trafficking. It also indicates the existence of an equilibrium between monomers and oligomers of this domain. In addition, the authors nicely illustrate the dependence of the hyperfine splitting on membrane depth.
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Biochemistry
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Zhang, Y.1
Shin, Y.K.2
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Zhang Y., Su Z., Zhang F., Chen Y., and Shin Y.K. A partially zipped SNARE complex stabilized by the membrane. J Biol Chem 280 (2005) 15595-15600
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Shin, Y.K.5
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61
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33646382407
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Conformational states and dynamics of rhodopsin in micelles and bilayers
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An outward tilt of transmembrane helix 6 of rhodopsin accompanies the phototransduction process. This work demonstrates that this structural change takes place in lipid bilayers and in micelles of dodecylmaltoside. It also nicely demonstrates that this structural change and optical changes in the chromophore are not directly coupled. Unlike the optical changes, the structural change is not strongly coupled to bilayer composition.
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Kusnetzow A.K., Altenbach C., and Hubbell W.L. Conformational states and dynamics of rhodopsin in micelles and bilayers. Biochemistry 45 (2006) 5538-5550. An outward tilt of transmembrane helix 6 of rhodopsin accompanies the phototransduction process. This work demonstrates that this structural change takes place in lipid bilayers and in micelles of dodecylmaltoside. It also nicely demonstrates that this structural change and optical changes in the chromophore are not directly coupled. Unlike the optical changes, the structural change is not strongly coupled to bilayer composition.
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(2006)
Biochemistry
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, pp. 5538-5550
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Kusnetzow, A.K.1
Altenbach, C.2
Hubbell, W.L.3
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62
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Effects of solubilization on the structure and function of the sensory rhodopsin II/transducer complex
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Klare J.P., Bordignon E., Doebber M., Fitter J., Kriegsmann J., Chizhov I., Steinhoff H.J., and Engelhard M. Effects of solubilization on the structure and function of the sensory rhodopsin II/transducer complex. J Mol Biol 356 (2006) 1207-1221
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Klare, J.P.1
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Kriegsmann, J.5
Chizhov, I.6
Steinhoff, H.J.7
Engelhard, M.8
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63
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EPR spectroscopic analysis of U7 hammerhead ribozyme dynamics during metal ion induced folding
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Edwards T.E., and Sigurdsson S.T. EPR spectroscopic analysis of U7 hammerhead ribozyme dynamics during metal ion induced folding. Biochemistry 44 (2005) 12870-12878
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Edwards, T.E.1
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Site-directed spin labeling studies reveal solution conformational changes in a GAAA tetraloop receptor upon Mg(2+)-dependent docking of a GAAA tetraloop
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Qin P.Z., Feigon J., and Hubbell W.L. Site-directed spin labeling studies reveal solution conformational changes in a GAAA tetraloop receptor upon Mg(2+)-dependent docking of a GAAA tetraloop. J Mol Biol 351 (2005) 1-8
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Identification of amino acids that promote specific and rigid TAR RNA-tat protein complex formation
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Edwards T.E., Robinson B.H., and Sigurdsson S.T. Identification of amino acids that promote specific and rigid TAR RNA-tat protein complex formation. Chem Biol 12 (2005) 329-337
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66
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22244435912
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Determination of the orientation of T4 lysozyme vectorially bound to a planar-supported lipid bilayer using site-directed spin labelling
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EPR spectra were obtained for spin-labeled T4 lysozyme mutants on single supported bilayers. The EPR spectra were analyzed using the stochastic Liouville equation approach of Freed and co-workers [20] and used to extract information on the protein orientation at the bilayer surface.
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Jacobsen K., Oga S., Hubbell W.L., and Risse T. Determination of the orientation of T4 lysozyme vectorially bound to a planar-supported lipid bilayer using site-directed spin labelling. Biophys J 88 (2005) 4351-4365. EPR spectra were obtained for spin-labeled T4 lysozyme mutants on single supported bilayers. The EPR spectra were analyzed using the stochastic Liouville equation approach of Freed and co-workers [20] and used to extract information on the protein orientation at the bilayer surface.
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Biophys J
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Jacobsen, K.1
Oga, S.2
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Details of the partial unfolding of T4 lysozyme on quartz using site-directed spin labeling
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Jacobsen K., Hubbell W.L., Ernst O.P., and Risse T. Details of the partial unfolding of T4 lysozyme on quartz using site-directed spin labeling. Angew Chem Int Ed Engl 45 (2006) 3874-3877
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Angew Chem Int Ed Engl
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68
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Crystal structures of spin labeled T4 lysozyme mutants: implications for the interpretation of EPR spectra in terms of structure
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Langen R., Oh K.J., Cascio D., and Hubbell W.L. Crystal structures of spin labeled T4 lysozyme mutants: implications for the interpretation of EPR spectra in terms of structure. Biochemistry 39 (2000) 8396-8405
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Langen, R.1
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69
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0037022173
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Structure and dynamics of a helical hairpin and loop region in annexin 12: a site-directed spin labeling study
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Isas J.M., Langen R., Haigler H.T., and Hubbell W.L. Structure and dynamics of a helical hairpin and loop region in annexin 12: a site-directed spin labeling study. Biochemistry 41 (2002) 1464-1473
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Isas, J.M.1
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Chiang Y.W., Borbat P.P., and Freed J.H. The determination of pair distance distributions by pulsed ESR using Tikhonov regularization. J Magn Reson 172 (2005) 279-295
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J Magn Reson
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Freed, J.H.3
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Maximum entropy: a complement to Tikhonov regularization for determination of pair distance distributions by pulsed ESR
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Chiang Y.W., Borbat P.P., and Freed J.H. Maximum entropy: a complement to Tikhonov regularization for determination of pair distance distributions by pulsed ESR. J Magn Reson 177 (2005) 184-196
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J Magn Reson
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Chiang, Y.W.1
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Freed, J.H.3
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72
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20544436458
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Use of EPR power saturation to analyze the membrane-docking geometries of peripheral proteins: applications to C2 domains
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Malmberg N.J., and Falke J.J. Use of EPR power saturation to analyze the membrane-docking geometries of peripheral proteins: applications to C2 domains. Annu Rev Biophys Biomol Struct 34 (2005) 71-90
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Annu Rev Biophys Biomol Struct
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, pp. 71-90
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Malmberg, N.J.1
Falke, J.J.2
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73
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33645098003
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A model system for investigating lineshape/structure correlations in RNA site-directed spin labeling
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EPR spectra of proteins have lineshapes that reflect local protein structure. This work demonstrates that RNA structural elements have unique spectral signatures. The authors establish a procedure to generate a library of EPR spectra for RNA.
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Qin P.Z., Iseri J., and Oki A. A model system for investigating lineshape/structure correlations in RNA site-directed spin labeling. Biochem Biophys Res Commun 343 (2006) 117-124. EPR spectra of proteins have lineshapes that reflect local protein structure. This work demonstrates that RNA structural elements have unique spectral signatures. The authors establish a procedure to generate a library of EPR spectra for RNA.
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(2006)
Biochem Biophys Res Commun
, vol.343
, pp. 117-124
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Qin, P.Z.1
Iseri, J.2
Oki, A.3
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74
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33745078551
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Reconstruction of the chemotaxis receptor-kinase assembly
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This work combines distance data obtained by EPR to define the complex between the chemotactic adaptor protein CheW and the histidine kinase CheA.
-
Park S.Y., Borbat P.P., Gonzalez-Bonet G., Bhatnagar J., Pollard A.M., Freed J.H., Bilwes A.M., and Crane B.R. Reconstruction of the chemotaxis receptor-kinase assembly. Nat Struct Mol Biol 13 (2006) 400-407. This work combines distance data obtained by EPR to define the complex between the chemotactic adaptor protein CheW and the histidine kinase CheA.
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(2006)
Nat Struct Mol Biol
, vol.13
, pp. 400-407
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Park, S.Y.1
Borbat, P.P.2
Gonzalez-Bonet, G.3
Bhatnagar, J.4
Pollard, A.M.5
Freed, J.H.6
Bilwes, A.M.7
Crane, B.R.8
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75
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33748352984
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Oldham WM, Van Eps N, Preininger AM, Hubbell WL, Hamm HE: Mechanism of the receptor-catalyzed activation of heterotrimeric G proteins. Nat Struct Mol Biol 2006, in press. Both CW EPR techniques and pulse methods are used to define structural changes in Gα that appear to be necessary for GDP release upon activation of the G protein by rhodopsin.
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76
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33748509727
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Xu Q, Ellena JF, Kim M, Cafiso DS: Substrate-dependent unfolding of the energy coupling motif of a membrane transport protein determined by double electron-electron resonance. Biochemistry 2006. in press. CW EPR indicates that the energy coupling motif in the outer membrane transport protein BtuB unfolds upon substrate binding. This work demonstrates, using pulse EPR techniques, that this energy coupling extends 20-30 Å into the periplasmic space during this conformational transition.
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