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Volumn 139, Issue 2, 1999, Pages 281-286

Nitroxide Side-Chain Dynamics in a Spin-Labeled Helix-Forming Peptide Revealed by High-Frequency (139.5-GHz) EPR Spectroscopy

Author keywords

Anisotropic motion; EPR; High frequency; Peptide; Side chain dynamics

Indexed keywords

PEPTIDE;

EID: 0033170414     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmre.1999.1769     Document Type: Article
Times cited : (17)

References (42)
  • 1
    • 0026783919 scopus 로고
    • Short alanine-based peptides may form 310-helices and not α-helices in aqueous solution
    • published correction appears in Nature 1995, 377, 257
    • S. M. Miick, G. V. Martinez, W. R. Fiori, A. P. Todd, and G. L Millhauser, Short alanine-based peptides may form 310-helices and not α-helices in aqueous solution [published correction appears in Nature 1995, 377, 257], Nature 359, 653-655 (1992).
    • (1992) Nature , vol.359 , pp. 653-655
    • Miick, S.M.1    Martinez, G.V.2    Fiori, W.R.3    Todd, A.P.4    Millhauser, G.L.5
  • 2
    • 0027435983 scopus 로고
    • 10-helix in alanine-based peptides: Evidence for a length-dependent structural transition
    • 10-helix in alanine-based peptides: Evidence for a length-dependent structural transition, Biochemistry 32, 11957-11962 (1993).
    • (1993) Biochemistry , vol.32 , pp. 11957-11962
    • Fiori, W.R.1    Miick, S.M.2    Millhauser, G.L.3
  • 3
    • 0028447414 scopus 로고
    • A single carboxy-terminal arginine determines the amino-terminal helix conformation of an alanine-based peptide
    • W. R. Fiori, K. M. Lundberg, and G. L. Millhauser, A single carboxy-terminal arginine determines the amino-terminal helix conformation of an alanine-based peptide, Nat. Struct. Biol. 1, 374-377 (1994).
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 374-377
    • Fiori, W.R.1    Lundberg, K.M.2    Millhauser, G.L.3
  • 4
    • 0028921182 scopus 로고
    • Views of helical peptides - A proposal for the position of 3(10)-helix along the thermodynamic folding pathway
    • G. L. Millhauser, Views of helical peptides - A proposal for the position of 3(10)-helix along the thermodynamic folding pathway, Biochemistry 34, 3873-3877 (1995).
    • (1995) Biochemistry , vol.34 , pp. 3873-3877
    • Millhauser, G.L.1
  • 5
    • 0026489966 scopus 로고
    • Selective placement of electron spin resonance spin labels: New structural methods for peptides and proteins
    • G. L. Millhauser, Selective placement of electron spin resonance spin labels: New structural methods for peptides and proteins, Trends Biochem. Sci. 17, 448-452 (1992).
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 448-452
    • Millhauser, G.L.1
  • 6
    • 0023683782 scopus 로고
    • The aggregation state of spin-labeled melittin in solution and bound to phospholipid membranes: Evidence that membrane-bound melittin is monomeric
    • C. Altenbach and W. L. Hubbell, The aggregation state of spin-labeled melittin in solution and bound to phospholipid membranes: Evidence that membrane-bound melittin is monomeric, Proteins 3, 230-242 (1988).
    • (1988) Proteins , vol.3 , pp. 230-242
    • Altenbach, C.1    Hubbell, W.L.2
  • 7
    • 0027219183 scopus 로고
    • Experimental molecular dynamics of an alanine-based helical peptide determined by spin label electron spin resonance
    • S. M. Miick, K. M. Casteel, and G. L. Millhauser, Experimental molecular dynamics of an alanine-based helical peptide determined by spin label electron spin resonance, Biochemistry 32, 8014-8021 (1993).
    • (1993) Biochemistry , vol.32 , pp. 8014-8021
    • Miick, S.M.1    Casteel, K.M.2    Millhauser, G.L.3
  • 8
    • 0028814090 scopus 로고
    • 3(10) Helices in peptides and proteins as studied by modified Zimm-Bragg theory
    • F. B. Sheinerman and C. L. Brooks, 3(10) Helices in peptides and proteins as studied by modified Zimm-Bragg theory, J. Am. Chem. Soc. 117, 10098-10103 (1995).
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 10098-10103
    • Sheinerman, F.B.1    Brooks, C.L.2
  • 9
    • 0029887269 scopus 로고    scopus 로고
    • A microscopic view of helix propagation - N and C-terminal helix growth in alanine helices
    • W. S. Young and C. L. Brooks, A microscopic view of helix propagation - N and C-terminal helix growth in alanine helices, J. Mol. Biol. 259, 560-572 (1996).
    • (1996) J. Mol. Biol. , vol.259 , pp. 560-572
    • Young, W.S.1    Brooks, C.L.2
  • 10
    • 0032558088 scopus 로고    scopus 로고
    • Biopolymer conformational distributions from solid-state NMR: Alpha-helix and 3(10)-helix contents of a helical peptide
    • H. W. Long and R. Tycko, Biopolymer conformational distributions from solid-state NMR: Alpha-helix and 3(10)-helix contents of a helical peptide, J. Am. Chem. Soc. 120, 7039-7048 (1998).
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 7039-7048
    • Long, H.W.1    Tycko, R.2
  • 11
    • 0025776471 scopus 로고
    • ESR spectra reflect local and global mobility in a short spin-labeled peptide throughout the α-helix → coil transition
    • A. P. Todd and G. L. Millhauser, ESR spectra reflect local and global mobility in a short spin-labeled peptide throughout the α-helix → coil transition, Biochemistry 30, 5515-5523 (1991).
    • (1991) Biochemistry , vol.30 , pp. 5515-5523
    • Todd, A.P.1    Millhauser, G.L.2
  • 12
    • 0025346254 scopus 로고
    • Transmembrane protein structure: Spin labeling of bacteriorhodopsin mutants
    • C. Altenbach, T. Marti, H. G. Khorana, and W. L. Hubbell, Transmembrane protein structure: spin labeling of bacteriorhodopsin mutants, Science 248, 1088-1092 (1990).
    • (1990) Science , vol.248 , pp. 1088-1092
    • Altenbach, C.1    Marti, T.2    Khorana, H.G.3    Hubbell, W.L.4
  • 13
    • 0028108981 scopus 로고
    • Investigation of structure and dynamics in membrane proteins using site-directed spin labeling
    • W. L. Hubbell and C. Altenbach, Investigation of structure and dynamics in membrane proteins using site-directed spin labeling, Curr. Opin. Struct. Biol. 4, 566-573 (1994).
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 566-573
    • Hubbell, W.L.1    Altenbach, C.2
  • 14
  • 15
    • 0002165192 scopus 로고
    • High-frequency and continuous-wave electron spin resonance
    • L. Kevan and M. K. Bowman, Eds., Wiley, New York
    • Y. S. Lebedev, High-frequency and continuous-wave electron spin resonance, in "Modern Pulsed and Continuous-Wave Electron Spin Resonance" (L. Kevan and M. K. Bowman, Eds.), pp. 365-404, Wiley, New York (1990).
    • (1990) Modern Pulsed and Continuous-Wave Electron Spin Resonance , pp. 365-404
    • Lebedev, Y.S.1
  • 17
    • 0020482581 scopus 로고
    • A novel reversible thiol-specific spin label: Papain active site labeling and inhibition
    • L. J. Berliner, J. Grunwald, H. O. Hankovszky, and K. Hideg, A novel reversible thiol-specific spin label: Papain active site labeling and inhibition, Anal. Biochem. 119, 450-455 (1982).
    • (1982) Anal. Biochem. , vol.119 , pp. 450-455
    • Berliner, L.J.1    Grunwald, J.2    Hankovszky, H.O.3    Hideg, K.4
  • 18
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • R. Koradi, M. Billeter, and K. Wuthrich, MOLMOL: A program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55 (1996).
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 20
    • 0002124244 scopus 로고
    • A spectrometer for dynamic nuclear polarization and electron paramagnetic resonance at high frequencies
    • L. R. Becerra, et al., A spectrometer for dynamic nuclear polarization and electron paramagnetic resonance at high frequencies, J. Magn. Reson. A 117, 28-40 (1995).
    • (1995) J. Magn. Reson. A , vol.117 , pp. 28-40
    • Becerra, L.R.1
  • 21
    • 0000408420 scopus 로고
    • Pulsed ENDOR spectroscopy in solids
    • L. Kevan and M. K. Bowman, Eds., Wiley-Interscience, New York
    • A. Grupp and M. Mehring, Pulsed ENDOR spectroscopy in solids, in "Modern Pulsed and Continuous-Wave Electron Spin Resonance" (L. Kevan and M. K. Bowman, Eds.) pp. 195-229, Wiley-Interscience, New York (1990).
    • (1990) Modern Pulsed and Continuous-Wave Electron Spin Resonance , pp. 195-229
    • Grupp, A.1    Mehring, M.2
  • 22
    • 0002319130 scopus 로고
    • Precision field-sweep system for superconducting solenoids and its application to high-frequency EPR spectroscopy
    • S. Un, J. Bryant and R. G. Griffin, Precision field-sweep system for superconducting solenoids and its application to high-frequency EPR spectroscopy, J. Magn. Reson. A 101, 92-94 (1993).
    • (1993) J. Magn. Reson. A , vol.101 , pp. 92-94
    • Un, S.1    Bryant, J.2    Griffin, R.G.3
  • 23
    • 33751386100 scopus 로고
    • Full determination of the rotational diffusion tensor by electron paramagnetic resonance at 250 GHz
    • D. E. Budil, K. A. Earle, and J. H. Freed, Full determination of the rotational diffusion tensor by electron paramagnetic resonance at 250 GHz, J. Phys. Chem. 97, 1294-1303 (1993).
    • (1993) J. Phys. Chem. , vol.97 , pp. 1294-1303
    • Budil, D.E.1    Earle, K.A.2    Freed, J.H.3
  • 24
    • 0001867405 scopus 로고
    • Chapter 1: Calculating slow motional magnetic resonance spectra: A user's guide
    • L. J. Berliner and J. Reuben, Eds., Plenum Press, New York
    • D. J. Schneider and J. H. Freed, Chapter 1: Calculating slow motional magnetic resonance spectra: A user's guide, in "Biological Magnetic Resonance: Spin Labeling Theory and Applications" (L. J. Berliner and J. Reuben, Eds.) Vol. 8, pp. 1-76, Plenum Press, New York (1989).
    • (1989) Biological Magnetic Resonance: Spin Labeling Theory and Applications , vol.8 , pp. 1-76
    • Schneider, D.J.1    Freed, J.H.2
  • 25
    • 0026657515 scopus 로고
    • Rotational diffusion and intermolecular collisions of a spin labeled a-helical peptide determined by electron spin resonance spectroscopy
    • S. M. Muck and G. L. Millhauser, Rotational diffusion and intermolecular collisions of a spin labeled a-helical peptide determined by electron spin resonance spectroscopy, Biophys. J. 63, 917-925 (1992).
    • (1992) Biophys. J. , vol.63 , pp. 917-925
    • Muck, S.M.1    Millhauser, G.L.2
  • 27
    • 0000953309 scopus 로고    scopus 로고
    • Electron spin resonance and structural analysis of water soluble, alanine-rich peptides incorporating TOAC
    • P. Hanson, et al., Electron spin resonance and structural analysis of water soluble, alanine-rich peptides incorporating TOAC, Mol. Phys. 95, 957-966 (1998).
    • (1998) Mol. Phys. , vol.95 , pp. 957-966
    • Hanson, P.1
  • 28
    • 0029758045 scopus 로고    scopus 로고
    • ESR characterization of hexameric, helical peptides using double TOAC spin labeling
    • P. Hanson, G. Millhauser, F. Formaggio, M. Crisma, and C. Toniolo, ESR characterization of hexameric, helical peptides using double TOAC spin labeling, J. Am. Chem. Soc. 118, 7618-7625 (1996).
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7618-7625
    • Hanson, P.1    Millhauser, G.2    Formaggio, F.3    Crisma, M.4    Toniolo, C.5
  • 29
    • 0030066039 scopus 로고    scopus 로고
    • Distinguishing helix conformations in alanine-rich peptides using the unnatural amino acid TOAC and electron spin resonance
    • P. Hanson, et al., Distinguishing helix conformations in alanine-rich peptides using the unnatural amino acid TOAC and electron spin resonance, J. Am. Chem. Soc. 118, 271-272 (1996).
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 271-272
    • Hanson, P.1
  • 30
    • 0029171261 scopus 로고
    • α,α-disubstituted glycine
    • α,α-disubstituted glycine, J. Pept. Sci. 1, 45-57 (1995).
    • (1995) J. Pept. Sci. , vol.1 , pp. 45-57
    • Toniolo, C.1
  • 31
    • 0002424797 scopus 로고
    • Deuteron NMR - A new tool for studying chain mobility and orientation in polymers
    • H. H. Kausch and H. G. Zachmann, Eds., Springer-Verlag, Berlin
    • H. W. Spiess, Deuteron NMR - A new tool for studying chain mobility and orientation in polymers, in "Advances in Polymer Science" (H. H. Kausch and H. G. Zachmann, Eds.) Vol. 66, pp. 23-58, Springer-Verlag, Berlin (1985).
    • (1985) Advances in Polymer Science , vol.66 , pp. 23-58
    • Spiess, H.W.1
  • 32
    • 0019724378 scopus 로고
    • 2H NMR line shapes for aromatic ring motion in solids
    • 2H NMR line shapes for aromatic ring motion in solids, J. Am. Chem. Soc. 103, 7707-7710 (1981).
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 7707-7710
    • Rice, D.M.1
  • 34
    • 0000894737 scopus 로고
    • Solid state NMR investigations of lipid bilayers, peptides and proteins
    • R. E. Sarma, Ed. Adenine Press, New York
    • D. M. Rice, et al., Solid state NMR investigations of lipid bilayers, peptides and proteins, in "Biomolecular Stereodynamics" (R. E. Sarma, Ed.) Vol. 2, pp. 255, Adenine Press, New York (1981).
    • (1981) Biomolecular Stereodynamics , vol.2 , pp. 255
    • Rice, D.M.1
  • 36
    • 33845378633 scopus 로고
    • Dynamics of phenylalanine in the solid state by NMR
    • M. H. Frey, J. A. DiVerdi, and S. J. Opella, Dynamics of phenylalanine in the solid state by NMR, J. Am. Chem. Soc. 107, 7311-7315 (1985).
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 7311-7315
    • Frey, M.H.1    DiVerdi, J.A.2    Opella, S.J.3
  • 37
    • 0029791152 scopus 로고    scopus 로고
    • Calculation of electron paramagnetic resonance spectra from Brownian dynamics trajectories -Application to nitroxide side chains in proteins
    • H. J. Steinhoff and W. L. Hubbell, Calculation of electron paramagnetic resonance spectra from Brownian dynamics trajectories -Application to nitroxide side chains in proteins, Biophys. J. 71, 2201-2212 (1996).
    • (1996) Biophys. J. , vol.71 , pp. 2201-2212
    • Steinhoff, H.J.1    Hubbell, W.L.2
  • 38
    • 0029905422 scopus 로고    scopus 로고
    • Motion of spin-labeled side chains in T4 lysozyme, correlation with protein structure and dynamics
    • H. S. Mchaourab, M. A. Lietzow, K. Hideg, and W. L. Hubbell, Motion of spin-labeled side chains in T4 lysozyme, correlation with protein structure and dynamics, Biochemistry 35, 7692-7704 (1996).
    • (1996) Biochemistry , vol.35 , pp. 7692-7704
    • Mchaourab, H.S.1    Lietzow, M.A.2    Hideg, K.3    Hubbell, W.L.4
  • 39
    • 0001945865 scopus 로고
    • Inhomogeneously broadened spin-label spectra
    • L. J. Berliner and J. Reuben, Eds., Plenum Press, New York
    • B. L. Bales, Inhomogeneously broadened spin-label spectra, in "Biological Magnetic Resonance: Spin Labeling Theory and Applications" (L. J. Berliner and J. Reuben, Eds.) Vol. 8, pp. 77-130, Plenum Press, New York (1989).
    • (1989) Biological Magnetic Resonance: Spin Labeling Theory and Applications , vol.8 , pp. 77-130
    • Bales, B.L.1
  • 40
    • 0001556604 scopus 로고
    • 250-GHz EPR of nitroxides in the slow-motional regime - Models of rotational diffusion
    • K. A. Earle, D. E. Budil, and J. H. Freed, 250-GHz EPR of nitroxides in the slow-motional regime - Models of rotational diffusion, J. Phys. Chem. 97, 13289-13297 (1993).
    • (1993) J. Phys. Chem. , vol.97 , pp. 13289-13297
    • Earle, K.A.1    Budil, D.E.2    Freed, J.H.3
  • 41
    • 0001634199 scopus 로고    scopus 로고
    • Aqueous sample holders for high-frequency electron spin resonance
    • J. Barnes and J. Freed, Aqueous sample holders for high-frequency electron spin resonance, Rev. Sci. Instrum. 68, 2838-2846 (1997).
    • (1997) Rev. Sci. Instrum. , vol.68 , pp. 2838-2846
    • Barnes, J.1    Freed, J.2
  • 42
    • 0040988793 scopus 로고
    • Interpretation and utilization for crystal structure determination of ESR spectra of single crystals of nitroxide free radicals
    • A. Capiomont, B. Chion, J. Lajzerowicz-Bonneteau, and H. Lemaire, Interpretation and utilization for crystal structure determination of ESR spectra of single crystals of nitroxide free radicals, J. Chem. Phys. 60, 2530-2535 (1974).
    • (1974) J. Chem. Phys. , vol.60 , pp. 2530-2535
    • Capiomont, A.1    Chion, B.2    Lajzerowicz-Bonneteau, J.3    Lemaire, H.4


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