Distance measurement between two flexible sites in proteins in high viscosity medium at physiological temperature using continuous wave EPR

[1]  E. Peterman,et al.  Förster resonance energy transfer and kinesin motor proteins. , 2014, Chemical Society reviews.

[2]  C. Tian,et al.  Efficient long-distance NMR-PRE and EPR-DEER restraints for two-domain protein structure determination , 2013, Protein & Cell.

[3]  C. Tian,et al.  Structural studies of Mycobacterium tuberculosis Rv0899 reveal a monomeric membrane-anchoring protein with two separate domains. , 2012, Journal of molecular biology.

[4]  U. Hellmich,et al.  NMR and EPR studies of membrane transporters , 2009, Biological chemistry.

[5]  Benoît Roux,et al.  Structural refinement of membrane proteins by restrained molecular dynamics and solvent accessibility data. , 2008, Biophysical journal.

[6]  G. Jeschke,et al.  Distance measurements in the borderline region of applicability of CW EPR and DEER: a model study on a homologous series of spin-labelled peptides. , 2008, Journal of magnetic resonance.

[7]  P. Fajer,et al.  Practical Pulsed Dipolar ESR (DEER) , 2007 .

[8]  W. Froncisz,et al.  Accessibility of nitroxide side chains: absolute Heisenberg exchange rates from power saturation EPR. , 2005, Biophysical journal.

[9]  P. Fajer,et al.  Explicit treatment of spin labels in modeling of distance constraints from dipolar EPR and DEER. , 2005, Journal of the American Chemical Society.

[10]  K. Hideg,et al.  Estimation of inter-residue distances in spin labeled proteins at physiological temperatures: experimental strategies and practical limitations. , 2001, Biochemistry.

[11]  G. Brudvig,et al.  Pulsed electron paramagnetic resonance methods for macromolecular structure determination. , 2001, Current opinion in structural biology.

[12]  A H Beth,et al.  Nitroxide spin-spin interactions: applications to protein structure and dynamics. , 1999, Annual review of biophysics and biomolecular structure.

[13]  W. Lehmann,et al.  Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[14]  H. Steinhoff,et al.  Determination of interspin distances between spin labels attached to insulin: comparison of electron paramagnetic resonance data with the X-ray structure. , 1997, Biophysical journal.

[15]  G. Buettner,et al.  Relationship of rotational correlation time from EPR spectroscopy and protein-membrane interaction , 1996 .

[16]  K. Hideg,et al.  Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics. , 1996, Biochemistry.

[17]  Y. Shin,et al.  Determination of the distance between two spin labels attached to a macromolecule. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[18]  H. Khorana,et al.  A collision gradient method to determine the immersion depth of nitroxides in lipid bilayers: application to spin-labeled mutants of bacteriorhodopsin. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[19]  J. Freed,et al.  Estimating slow-motional rotational correlation times for nitroxides by electron spin resonance , 1972 .