Molecular distances from dipolar coupled spin-labels: The global analysis of multifrequency continuous wave electron paramagnetic resonance data

Biophysical Journal

Volumn 72, Issue 4, 1997, Pages 1861-1877

  Hustedt, Eric J ^a   Smirnov, Alex I ^b   Laub, Charles F ^a   Cobb, Charles E ^a   Beth, Albert H ^a,c  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^c VANDERBILT UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANALYTIC METHOD; ARTICLE; ELECTRON SPIN RESONANCE; IMMOBILIZED CELL; MEMBRANE BINDING; MOLECULAR DYNAMICS; MOLECULAR MODEL; NONHUMAN; PROTEIN DOMAIN; PROTEIN QUATERNARY STRUCTURE; SITE DIRECTED MUTAGENESIS;

EID: 0030950516     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78832-5     Document Type: Article

References (46)

1. Altenbach, C., T. Marti, H. Gobind Khorana, and W. L. Hubbell. 1990. Transmembrane protein structure: spin labeling of bacteriorhodopsin mutants. Science. 248:1088-1092.
2. Beechem, J. M., E. Gratton, M. Ameloot, J. R. Knutson, and L. Brand. 1991. The global analysis of fluorescence intensity and anisotropy decay data: second generation theory and programs. In Topics in Fluorescence Spectroscopy, Vol. 2: Principles. J. R. Lakowicz, editor. Plenum Press, New York. 241-305.
3. Berliner, L. J. 1970. Refinement and location of the hydrogen atoms in the nitroxide 2,2,6,6-tetramethyl-4-piperidinol-1-oxyl. Acta Crystallogr. B. B26:1198-1202.
4. 15N] nitroxide spin labels. Effects of noncoincident magnetic and diffusion tensor principal axes. J. Phys. Chem. 87:359-367.
5. + bound to glyceraldehyde-3-phosphate dehydrogenase: comparison of EPR and X-ray modeling data. J. Biol. Chem. 259:9717-9728.
6. 2H-substituted maleimide spin-labels: improved sensitivity and resolution for biological EPR studies. Proc. Natl. Acad. Sci. U.S.A. 78:967-971.
7. Dalton, L. R. 1985. EPR and Advanced EPR Studies of Biological Systems. CRC Press, Boca Raton, FL. 314 pp.
8. + derivatives. Biochim. Biophys. Acta. 659:422-433.
9. Eaton, S. S., and G. R. Eaton. 1989. Resolved electron-electron spin-spin splittings in EPR spectra. In Biological Magnetic Resonance, Vol. 8: Spin Labeling Theory and Applications, L. J. Berliner and J. Reuben, editors. Plenum Press, New York. 340-398.
10. Eaton, S. S., K. M. More, D. L. DuBois, P. M. Boymel, and G. R. Eaton. 1980. Metal-nitroxyl interactions. 15. Comparison of EPR spectra at X band and Q band. J. Magn. Reson. 41:150-157.
11. Eaton, S. S., K. M. More, B. M. Sawant, P. M. Boymel, and G. R. Eaton. 1983. Metal-nitroxyl interactions. 29. EPR studies of spin-labeled copper complexes in frozen solution. J. Magn. Reson. 52:435-449.
12. Farahbakhsh, Z. T., K. D. Ridge, H. G. Khorana, and W. L. Hubbell. 1995. Mapping light-dependent structural changes in the cytoplasmic loop connecting helices C and D in rhodopsin: a site-directed spin labeling study. Biochemistry. 34:8812-8819.
13. Freed, J. 1976. Theory of slow tumbling ESR spectra for nitroxides. In Spin Labeling: Theory and Applications. L. J. Berliner, editor. Academic Press, New York. 53-132.
14. Hanson, P., G. Martinez, G. Millhauser, F. Formaggio, M. Crisma, C. Toniolo, and C. Vita. 1996a. Distinguishing helix conformations in alanine-rich peptides using the unnatural amino acid TOAC and electron spin resonance. J. Am. Chem. Soc. 118:271-272.
15. Hanson, P., G. Millhauser, F. Formaggio, M. Crisma, and C. Toniolo. 1996b. ESR characterization of hexameric, helical peptides using double TOAC spin labeling. J. Am. Chem. Soc. 118:7618-7625.
16. Hubbell, W. L., and C. Altenbach. 1994. Site-directed spin labeling of membrane proteins. In Membrane Protein Structure: Experimental Approaches. S. H. White, editor. Oxford University Press, New York. 224-248.
17. Hubbell, W. L., H. S. Mchaourab, C. Altenbach, and M. A. Lietzow. 1996. Watching proteins move using site-directed spin labeling. Structure. 4:779-783.
18. Hustedt, E. J., C. E. Cobb, A. H. Beth, and J. M. Beechem. 1993. Measurement of rotational dynamics by the simultaneous nonlinear analysis of optical and EPR data. Biophys. J. 64:614-621.
19. Hyde, J. S., M. E. Newton, R. A. Strangeway, J. G Camenisch, and W. Froncisz. 1991. Rev. Sci. Instrum. 32:2969-2975.
20. Jost, P., and O. H. Griffith. 1972. Electron spin resonance and the spin labeling method. In Methods in Pharmacology, Vol. 2. C. F. Chignell, editor. Appleton-Century-Crofts, New York. 223-276.
21. Larsen, R. G., and D. J. Singel. 1993. Double electron-electron resonance spin-echo modulation: spectroscopic measurement of electron spin pair separations in orientationally disordered solids. J. Chem. Phys. 98: 5134-5146.
22. Liu, J., J. M. Rutz, P. E. Klebba, and J. B. Feix. 1994. A site-directed spin-labeling study of ligand induced conformational changes in the ferric enterobactin receptor, Fep A. Biochemistry. 33:13274-13283.
23. Luckhurst, G. R. 1976. Biradicals as spin probes. In Spin Labeling: Theory and Applications. L. J. Berliner, editor. Academic Press, New York. 133-181.
24. Mchaourab, H. S., M. A. Lietzow, K. Hideg, and W. L. Hubbell. 1996. Motion of spin-labeled side chains in T4 lysozyme. correlation with protein structure and dynamics. Biochemistry. 35:7692-7704.
25. Mercer, W. D., S. I. Winn, and H. C. Watson. 1976. Twinning in crystals of human skeletal muscle D-glyceraldehyde-3-phosphate dehydrogenase. J. Mol. Biol. 104:277-283.
26. 10-helices, and not α-helices in aqueous solution. Nature. 359:653-655.
27. Millhauser, G. L. 1992. Selective placement of electron spin resonance spin labels: new structural methods for proteins and peptides. Trends in Biochem. Sci. 17:448-452.
28. Moras, D., K. W. Olsen, M. N. Sabesan, M. Buehner, G. C. Ford, and M. G. Rossmann. 1975. Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 250:9137-9162.
29. Oh, K. J., H. Zhan, C. Cui, K. Hideg, R. J. Collier, and W. L. Hubbell. 1996. Organization of diphtheria toxin T domain in bilayers: a site-directed spin labeling study. Science. 273:810-812.
30. 15N and deuterium spin probes for biomedical electron paramagnetic resonance investigations. In Biological Magnetic Resonance, Vol. 8: Spin Labeling Theory and Applications. L. J. Berliner and J. Reuben, editors. Plenum Press, New York. 547-595.
31. Pfannebecker, V., H. Klos, M. Hubrich, T. Volkmer, A. Heuer, U. Wiesner, and H. W. Spiess. 1996. Determination of end-to-end distances in oligomers by pulsed EPR. J. Phys. Chem. 100:13428-13432.
32. Press, W. H., S. A. Teukolsky, W. T. Vetterling, and B. P. Flannery. 1992. Numerical Recipes in FORTRAN: The Art of Scientific Computing. Cambridge University Press, New York. 963 pp.
33. Rabenstein, M. D., and Y.-K. Shin. 1995. Determination of the distance between two spin labels attached to a macromolecule. Proc. Natl. Acad. Sci. U.S.A. 92:8239-8243.
34. Raitsimring, A., J. Peisach, H. C. Lee, and X. Chen. 1992. Measurement of distance distribution between spin labels in spin-labeled hemoglobin using an electron spin echo method. J. Phys. Chem. 96:3526-3531.
35. Rakowsky, M. H., K. M. More, A. V. Kulikov, G. R. Eaton, and S. S. Eaton. 1995. Time-domain electron paramagnetic resonance as a probe of electron-electron spin-spin interaction in spin-labeled low-spin iron porphyrins. J. Am. Chem. Soc. 117:2049-2057.
36. Robinson, B. H., L. Slutsky, and F. Auteri. 1992. Direct simulation of continuous wave electron paramagnetic resonance spectra from Brownian dynamics trajectories. J. Chem. Phys. 96:2609-2616.
37. Saxena, S., and J. H. Freed. 1996. Double quantum two-dimensional Fourier transform electron spin resonance: distance measurements. Chem. Phys. Lett. 251:102-110.
38. Schneider, D. J., and J. H. Freed. 1989. Calculating slow motional magnetic resonance spectra: a user's guide. In Biological Magnetic Resonance, Vol. 8: Spin Labeling Theory and Applications. L. J. Berliner and J. Reuben, editors. Plenum Press, New York. 1-76.
39. Shin, Y.-K., C. Levinthal, F. Levinthal, and W. L. Hubbell. 1993. Colicin E1 binding to membranes: time-resolved studies of spin labeled mutants. Science. 259:960-963.
40. Smirnov, A. I., T. I. Smirnova, and P. D. Morse II. 1995. Very high frequency electron paramagnetic resonance of 2,2,6,6-tetramethyl-1-piperidinyloxy in 1,2-dipalmitoyl-sn-glycero-3-phosphatidylcholine liposomes: partitioning and molecular dynamics. Biophys. J. 68:2350-2360.
41. Steinhoff, H.-J., and W. L. Hubbell. 1996. Calculation of electron paramagnetic resonance spectra from Brownian dynamics trajectories: application to nitroxide side chains in proteins. Biophys. J. 71:2201-2212.
42. van der Meer, B. W., M. A. Raymer, S. L. Wagoner, R. L. Hackney, J. M. Beechem, and E. Gratton. 1993. Designing matrix models for fluorescence energy transfer between moving donors and acceptors. Biophys. J. 64:1243-1263.
43. Voss, J., M. M. He, W. L. Hubbell, and H. R. Kaback. 1996. Site-directed spin labeling demonstrates that transmembrane domain XII in the lactose permease of Escherichia coli is an α-helix. Biochemistry. 35: 12915-12918.
44. Voss, J., L. Salwinski, H. R. Kabach, and W. L. Hubbell. 1995a. A method for distance determination in proteins using a designed metal ion binding site and site-directed spin labeling: evaluation with T4 lysozyme. Proc. Natl. Acad. Sci. U.S.A. 92:12295-12299.
45. Voss, J., W. L. Hubbell, and H. R. Kabach. 1995b. Distance determination in proteins using designed metal ion binding sites and site-directed spin labeling: application to the lactose permease of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 92:12300-12304.
46. Wang, W., R. L. Belford, R. B. Clarkson, P. H. Davis, J. Forrer, M. J. Nilges, M. D. Timken, T. Walczak, M. C. Thurnauer, J. R. Norris, A. L. Morris, and Y. Zwang. 1994. Very high frequency EPR-94 GHz instrument and applications to primary reaction centers from photosynthetic red bacteria and to other disordered systems. Appl. Magn. Reson. 6:195-215.