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Volumn 232, Issue , 2013, Pages 53-61

Structure and dynamics of an imidazoline nitroxide side chain with strongly hindered internal motion in proteins

Author keywords

Spin labeling

Indexed keywords

CHAINS; CRYSTAL ATOMIC STRUCTURE; ELECTRON RESONANCE; ELECTRON SPIN RESONANCE SPECTROSCOPY; PARAMAGNETIC RESONANCE; PROTEINS; QUANTUM THEORY; SPIN FLUCTUATIONS; SULFUR COMPOUNDS;

EID: 84877846721     PISSN: 10907807     EISSN: 10960856     Source Type: Journal    
DOI: 10.1016/j.jmr.2013.04.013     Document Type: Article
Times cited : (40)

References (61)
  • 1
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • W.L. Hubbell, D.S. Cafiso, C. Altenbach, Identifying conformational changes with site-directed spin labeling, Nat. Struct. Mol. Biol. 7 (2000) 735-739.
    • (2000) Nat. Struct. Mol. Biol. , vol.7 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 2
    • 67749124074 scopus 로고    scopus 로고
    • Osmolyte perturbation reveals conformational equilibria in spin-labeled proteins
    • C.J. Lopez, M.R. Fleissner, Z. Guo, A.K. Kusnetzow, W.L. Hubbell, Osmolyte perturbation reveals conformational equilibria in spin-labeled proteins, Protein Sci. 18 (2009) 1637-1652.
    • (2009) Protein Sci. , vol.18 , pp. 1637-1652
    • Lopez, C.J.1    Fleissner, M.R.2    Guo, Z.3    Kusnetzow, A.K.4    Hubbell, W.L.5
  • 3
    • 84865410842 scopus 로고    scopus 로고
    • Mapping molecular flexibility of proteins with site-directed spin labeling: A case study of myoglobin
    • C.J. Lopez, S. Oga, W.L. Hubbell, Mapping molecular flexibility of proteins with site-directed spin labeling: a case study of myoglobin, Biochemistry 51 (2012) 6568-6583.
    • (2012) Biochemistry , vol.51 , pp. 6568-6583
    • Lopez, C.J.1    Oga, S.2    Hubbell, W.L.3
  • 4
    • 84867575393 scopus 로고    scopus 로고
    • Ligand-induced structural changes in the E. Coli ferric citrate transporter reveal modes for regulating protein-protein interactions
    • A. Mokdad, D.Z. Herrick, A.K. Kahn, E. Andrews, M. Kim, Ligand-induced structural changes in the E. Coli ferric citrate transporter reveal modes for regulating protein-protein interactions, J. Mol. Biol. 423 (2012) 818-830.
    • (2012) J. Mol. Biol. , vol.423 , pp. 818-830
    • Mokdad, A.1    Herrick, D.Z.2    Kahn, A.K.3    Andrews, E.4    Kim, M.5
  • 6
    • 0036606899 scopus 로고    scopus 로고
    • A new spin on protein dynamics
    • DOI 10.1016/S0968-0004(02)02095-9, PII S0968000402020959
    • L. Columbus, W.L. Hubbell, A new spin on protein dynamics, Trends Biochem. Sci. 27 (2002) 288-295. (Pubitemid 34628668)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.6 , pp. 288-295
    • Columbus, L.1    Hubbell, W.L.2
  • 7
    • 2942527068 scopus 로고    scopus 로고
    • Mapping backbone dynamics in solution with site-directed spin labeling: GCN4-58 bZip free and bound to DNA
    • DOI 10.1021/bi0497906
    • L. Columbus, W.L. Hubbell, Mapping backbone dynamics in solution with site directed spin labeling: GCN4-58 bZip free and bound to DNA, Biochemistry 43 (2004) 7273-7287. (Pubitemid 38745748)
    • (2004) Biochemistry , vol.43 , Issue.23 , pp. 7273-7287
    • Columbus, L.1    Hubbell, W.L.2
  • 8
    • 71149088976 scopus 로고    scopus 로고
    • Resolving conformational and rotameric exchange in spin-labeled proteins using saturation recovery EPR
    • M.D. Bridges, K. Hideg, W.L. Hubbell, Resolving conformational and rotameric exchange in spin-labeled proteins using saturation recovery EPR, Appl. Magn. Reson. 37 (2010) 363-390.
    • (2010) Appl. Magn. Reson. , vol.37 , pp. 363-390
    • Bridges, M.D.1    Hideg, K.2    Hubbell, W.L.3
  • 10
    • 0024809884 scopus 로고
    • Site-directed mutagenesis of colicin E1 provides specific attachment sites for spin labels whose spectra are sensitive to local conformation
    • A. Todd, V. Crozel, F. Levinthal, C. Levinthal, W.L. Hubbell, Site-directed mutagenesis of colicin E1 provides specific attachment sites for spin labels whose spectra are sensitive to local conformation, Proteins: Struct., Funct., Genet. 6 (1989) 294.
    • (1989) Proteins: Struct., Funct., Genet. , vol.6 , pp. 294
    • Todd, A.1    Crozel, V.2    Levinthal, F.3    Levinthal, C.4    Hubbell, W.L.5
  • 11
    • 0035799354 scopus 로고    scopus 로고
    • Molecular motion of spin labeled side chains in α-helices: Analysis by variation of side chain structure
    • DOI 10.1021/bi002645h
    • L. Columbus, T. Kalai, J. Jeko, K. Hideg, W.L. Hubbell, Molecular motion of spin labeled side chains in alpha-helices: analysis by variation of side chain structure, Biochemistry 40 (2001) 3828-3846. (Pubitemid 32280420)
    • (2001) Biochemistry , vol.40 , Issue.13 , pp. 3828-3846
    • Columbus, L.1    Kalai, T.2    Jeko, J.3    Hideg, K.4    Hubbell, W.L.5
  • 14
    • 0029905422 scopus 로고    scopus 로고
    • Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics
    • DOI 10.1021/bi960482k
    • H.S. Mchaourab, M.A. Lietzow, K. Hideg, W.L. Hubbell, Motion of spin-labeled side chains in T4 Lysozyme. Correlation with protein structure and dynamics, Biochemistry 35 (1996) 7692-7704. (Pubitemid 26202511)
    • (1996) Biochemistry , vol.35 , Issue.24 , pp. 7692-7704
    • Mchaourab, H.S.1    Lietzow, M.A.2    Hideg, K.3    Hubbell, W.L.4
  • 15
    • 0039171268 scopus 로고    scopus 로고
    • Crystal structures of spin labeled T4 lysozyme mutants: Implications for the interpretation of EPR spectra in terms of structure
    • DOI 10.1021/bi000604f
    • R. Langen, K.J. Oh, D. Cascio, W.L. Hubbell, Crystal structures of spin labeled T4 Lysozyme mutants: implications for the interpretation of EPR spectra in terms of structure, Biochemistry 39 (2000) 8396-8405. (Pubitemid 30489936)
    • (2000) Biochemistry , vol.39 , Issue.29 , pp. 8396-8405
    • Langen, R.1    Oh, K.J.2    Cascio, D.3    Hubbell, W.L.4
  • 16
    • 34249794011 scopus 로고    scopus 로고
    • Structural determinants of nitroxide motion in spin-labeled proteins: Tertiary contact and solvent-inaccessible sites in helix G of T4 lysozyme
    • DOI 10.1110/ps.062739107
    • Z. Guo, D. Cascio, K. Hideg, T. Kalai, W.L. Hubbell, Structural determinants of nitroxide motion in spin-labeled proteins: tertiary contact and solventinaccessible sites in helix G of T4 Lysozyme, Protein Sci. 16 (2007) 1069-1086. (Pubitemid 46849217)
    • (2007) Protein Science , vol.16 , Issue.6 , pp. 1069-1086
    • Guo, Z.1    Cascio, D.2    Hideg, K.3    Kalai, T.4    Hubbell, W.L.5
  • 17
    • 38649125853 scopus 로고    scopus 로고
    • Structural determinants of nitroxide motion in spin-labeled proteins: Solvent-exposed sites in helix B of T4 lysozyme
    • DOI 10.1110/ps.073174008
    • Z. Guo, D. Cascio, K. Hideg, W.L. Hubbell, Structural determinants of nitroxide motion in spin-labeled proteins: solvent-exposed sites in helix B of T4 Lysozyme, Protein Sci. 17 (2008) 228-239. (Pubitemid 351171835)
    • (2008) Protein Science , vol.17 , Issue.2 , pp. 228-239
    • Guo, Z.1    Cascio, D.2    Hideg, K.3    Hubbell, W.L.4
  • 18
    • 65649117362 scopus 로고    scopus 로고
    • Structural origin of weakly ordered nitroxide motion in spin-labeled proteins
    • M.R. Fleissner, D. Cascio, W.L. Hubbell, Structural origin of weakly ordered nitroxide motion in spin-labeled proteins, Protein Sci. 18 (2009) 893-908.
    • (2009) Protein Sci. , vol.18 , pp. 893-908
    • Fleissner, M.R.1    Cascio, D.2    Hubbell, W.L.3
  • 19
    • 0033000691 scopus 로고    scopus 로고
    • A multifrequency electron spin resonance study of T4 lysozyme dynamics
    • J.P. Barnes, Z. Liang, H.S. Mchaourab, J.H. Freed, W.L. Hubbell, A multi frequency electron spin resonance study of T4 Lysozyme dynamics, Biophys. J. 76 (1999) 3298-3306. (Pubitemid 29269477)
    • (1999) Biophysical Journal , vol.76 , Issue.6 , pp. 3298-3306
    • Barnes, J.P.1    Liang, Z.2    Mchaourab, H.S.3    Freed, J.H.4    Hubbell, W.L.5
  • 21
    • 85027955226 scopus 로고    scopus 로고
    • Protein structure and dynamics revealed by site directed spin labeling and multi frequency EPR
    • Y.E. Nesmelov, D.D. Thomas, Protein structure and dynamics revealed by site directed spin labeling and multi frequency EPR, Biophys. Rev. 2 (2010) 91-99.
    • (2010) Biophys. Rev. , vol.2 , pp. 91-99
    • Nesmelov, Y.E.1    Thomas, D.D.2
  • 22
    • 84865127288 scopus 로고    scopus 로고
    • High-resolution structure of a protein spin-label in a solvent-exposed b-sheet and comparison with DEER spectroscopy
    • T.M. Cunningham, M.S. McGoff, I. Sengupta, C.P. Jaroniec, S.W. Horne, S. Saxena, High-resolution structure of a protein spin-label in a solvent-exposed b-sheet and comparison with DEER spectroscopy, Biochemistry 51 (2012) 6350-6359.
    • (2012) Biochemistry , vol.51 , pp. 6350-6359
    • Cunningham, T.M.1    McGoff, M.S.2    Sengupta, I.3    Jaroniec, C.P.4    Horne, S.W.5    Saxena, S.6
  • 23
    • 80054730815 scopus 로고    scopus 로고
    • Molecular origin of electron paramagnetic resonance line shapes on b-barrel membrane proteins: The local solvation environment modulates spin-label configuration
    • D.M. Freed, A.K. Khan, P.S. Horanyi, D.S. Cafiso, Molecular origin of electron paramagnetic resonance line shapes on b-barrel membrane proteins: the local solvation environment modulates spin-label configuration, Biochemistry 50 (2011) 8792-8803.
    • (2011) Biochemistry , vol.50 , pp. 8792-8803
    • Freed, D.M.1    Khan, A.K.2    Horanyi, P.S.3    Cafiso, D.S.4
  • 24
    • 78649504797 scopus 로고    scopus 로고
    • Structural origins of nitroxide side chain dynamics on membrane protein a-helical sites
    • B.M. Kroncke, P.S. Horanyi, L. Columbus, Structural origins of nitroxide side chain dynamics on membrane protein a-helical sites, Biochemistry 49 (2010) 10045-10060.
    • (2010) Biochemistry , vol.49 , pp. 10045-10060
    • Kroncke, B.M.1    Horanyi, P.S.2    Columbus, L.3
  • 25
    • 78651466789 scopus 로고    scopus 로고
    • Conformational analysis of a nitroxide side chain in an a-helix with density functional theory
    • D. Toledo Warshaviak, L. Serbulea, K.N. Houk, W.L. Hubbell, Conformational analysis of a nitroxide side chain in an a-helix with density functional theory, J. Phys. Chem. B 115 (2011) 397-405.
    • (2011) J. Phys. Chem. B , vol.115 , pp. 397-405
    • Warshaviak, D.T.1    Serbulea, L.2    Houk, K.N.3    Hubbell, W.L.4
  • 28
    • 27744496802 scopus 로고    scopus 로고
    • Expressed protein ligation to study protein interactions: Semi-synthesis of the G-protein alpha subunit
    • DOI 10.2174/0929866054864175
    • L.L. Anderson, G.R. Marshall, T.J. Baranski, Expressed protein ligation to study protein interactions: semi-synthesis of the G-protein alpha subunit, Protein Pept. Lett. 12 (2005) 783-787. (Pubitemid 41634858)
    • (2005) Protein and Peptide Letters , vol.12 , Issue.8 , pp. 783-787
    • Anderson, L.L.1    Marshall, G.R.2    Baranski, T.J.3
  • 29
    • 33646374402 scopus 로고    scopus 로고
    • Orientation of TOAC amino-acid spin labels in alpha-helices and beta-strands
    • D.J. Marsh, Orientation of TOAC amino-acid spin labels in alpha-helices and beta-strands, J. Magn. Reson. 180 (2006) 305-310.
    • (2006) J. Magn. Reson. , vol.180 , pp. 305-310
    • Marsh, D.J.1
  • 30
    • 35348980142 scopus 로고    scopus 로고
    • Rotational dynamics of phospholamban determined by multifrequency electron paramagnetic resonance
    • DOI 10.1529/biophysj.107.108910
    • Y.E. Nesmelov, C.B. Karim, L. Song, P.G. Fajer, D.D. Thomas, Rotational dynamics of phospholamban determined by multifrequency electron paramagnetic resonance, Biophys. J. 93 (2007) 2805-2812. (Pubitemid 47607816)
    • (2007) Biophysical Journal , vol.93 , Issue.8 , pp. 2805-2812
    • Nesmelov, Y.E.1    Karim, C.B.2    Song, L.3    Fajer, P.G.4    Thomas, D.D.5
  • 31
    • 77955583625 scopus 로고    scopus 로고
    • Electron paramagnetic resonance studies of functionally active, nitroxide spin-labeled peptide analogues of the C-terminus of a G-protein a subunit
    • N. Van Eps, L.L. Anderson, O.G. Kisselev, T.J. Baranski, W.L. Hubbell, G.R. Marshall, Electron paramagnetic resonance studies of functionally active, nitroxide spin-labeled peptide analogues of the C-terminus of a G-protein a subunit, Biochemistry 49 (2010) 6877-6886.
    • (2010) Biochemistry , vol.49 , pp. 6877-6886
    • Eps, N.V.1    Anderson, L.L.2    Kisselev, O.G.3    Baranski, T.J.4    Hubbell, W.L.5    Marshall, G.R.6
  • 32
    • 0029115328 scopus 로고
    • Determination of the distance between two spin labels attached to a macromolecule
    • M.D. Rabenstein, Y.K. Shin, Determination of the distance between two spin labels attached to a macromolecule, Proc. Natl. Acad. Sci. USA 92 (1995) 8239- 8243.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8239-8243
    • Rabenstein, M.D.1    Shin, Y.K.2
  • 33
    • 0035951101 scopus 로고    scopus 로고
    • Estimation of inter-residue distances in spin labeled proteins at physiological temperatures: Experimental strategies and practical limitations
    • DOI 10.1021/bi011544w
    • C. Altenbach, K.J. Oh, R.J. Trabanino, K. Hideg, W.L. Hubbell, Estimation of interresidue distances in spin labeled proteins at physiological temperatures: experimental strategies and practical limitations, Biochemistry 40 (2001) 15471-15482. (Pubitemid 34015174)
    • (2001) Biochemistry , vol.40 , Issue.51 , pp. 15471-15482
    • Altenbach, C.1    Oh, K.-J.2    Trabanino, R.J.3    Hideg, K.4    Hubbell, W.L.5
  • 34
    • 0037112592 scopus 로고    scopus 로고
    • Distance measurements in the nanometer range by pulse EPR
    • G. Jeschke, Distance measurements in the nanometer range by pulse EPR, Chem Phys Chem 3 (2002) 927-932.
    • (2002) Chem Phys Chem , vol.3 , pp. 927-932
    • Jeschke, G.1
  • 35
    • 34548317408 scopus 로고    scopus 로고
    • Long-range distance determinations in biomacromolecules by EPR spectroscopy
    • DOI 10.1017/S003358350700460X
    • O. Schiemann, T.F. Prisner, Long-range distance determinations in biomolecules by EPR spectroscopy, Q. Rev. Biophys. 40 (2007) 1-53. (Pubitemid 47343581)
    • (2007) Quarterly Reviews of Biophysics , vol.40 , Issue.1 , pp. 1-53
    • Schiemann, O.1    Prisner, T.F.2
  • 36
    • 0024424225 scopus 로고
    • Quantitative determination of SH groups in low- and high-molecular-weight compounds by an electron spin resonance method
    • V.V. Khramtsov, V.I. Yelinova, L.M. Weiner, T.A. Berezina, V.V. Martin, L.B. Volodarsky, Quantitative determination of SH groups in low- and highmolecular- weight compounds by an electron spin resonance method, Anal. Biochem. 182 (1989) 58-63. (Pubitemid 19251282)
    • (1989) Analytical Biochemistry , vol.182 , Issue.1 , pp. 58-63
    • Khramtsov, V.V.1    Yelinova, V.I.2    Weiner, L.M.3    Berezina, T.A.4    Martin, V.V.5    Volodarsky, L.B.6
  • 37
    • 0000326938 scopus 로고    scopus 로고
    • Nonlinear-least-squares analysis of slow-motion EPR spectra in one and two dimensions using a modified levenberg-marquardt algorithm
    • D.E. Budil, S. Lee, S. Saxena, J.H. Freed, Nonlinear least-squares analysis of slow motional EPR spectra in one and two dimensions using a modified Levenberg- Marquardt algorithm, J. Magn. Reson. A 120 (1996) 155-189. (Pubitemid 126751752)
    • (1996) Journal of Magnetic Resonance - Series A , vol.120 , Issue.2 , pp. 155-189
    • Budil, D.E.1    Sanghyuk, L.2    Saxena, S.3    Freed, J.H.4
  • 39
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, W. Minor, Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol. 276 (1996) 307-326.
    • (1996) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 40
    • 0023104358 scopus 로고
    • Structure of bacteriophage T4 lysozyme refined at 1.7 Å resolution
    • L.H. Weaver, B.W. Matthews, Structure of bacteriophage T4 Lysozyme refined at 1.7 Å resolution, J. Mol. Biol. 193 (1987) 189-199. (Pubitemid 17228125)
    • (1987) Journal of Molecular Biology , vol.193 , Issue.1 , pp. 189-199
    • Weaver, L.H.1    Matthews, B.W.2
  • 42
    • 0034730423 scopus 로고    scopus 로고
    • Size versus polarizability in protein-ligand interactions: Binding of noble gases within engineered cavities in phage T4 Lysozyme
    • M.L. Quillin, W.A. Breyer, I.J. Griswold, B.W. Matthews, Size versus polarizability in protein-ligand interactions: binding of noble gases within engineered cavities in phage T4 Lysozyme, J. Mol. Biol. 302 (2000) 955-977.
    • (2000) J. Mol. Biol. , vol.302 , pp. 955-977
    • Quillin, M.L.1    Breyer, W.A.2    Griswold, I.J.3    Matthews, B.W.4
  • 46
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • R.A. Laskowski, M.W. MacArthur, D.S. Moss, J.M. Thornton, PROCHECK: a program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26 (1993) 283-291.
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 47
    • 0027180507 scopus 로고
    • Verification of protein structures: Patterns of nonbonded atomic interactions
    • C. Colovos, T.O. Yeates, Verification of protein structures: patterns of nonbonded atomic interactions, Protein Sci. 2 (1993) 1511-1519. (Pubitemid 23262844)
    • (1993) Protein Science , vol.2 , Issue.9 , pp. 1511-1519
    • Colovos, C.1    Yeates, T.O.2
  • 49
    • 0029024759 scopus 로고
    • Quantitative determination of thiol groups in low and high molecular weight compounds by electron paramagnetic resonance
    • L.M. Weiner, Quantitative determination of thiol groups in low and high molecular weight compounds by electron paramagnetic resonance, Methods Enzymol. 251 (1995) 87-105.
    • (1995) Methods Enzymol , vol.251 , pp. 87-105
    • Weiner, L.M.1
  • 50
    • 0030611256 scopus 로고    scopus 로고
    • Quantitative determinatin and reversible modification of thiols using imidazolidine biradica disulfide label
    • DOI 10.1016/S0165-022X(97)00035-3, PII S0165022X97000353
    • V.V. Khramtsov, V.I. Yelinova, Y.I. Glazachev, V.A. Reznikov, G. Zimmer, Quantitative determination and reversible modification of thiols using imidazolidine biradical disulfide label, J. Biochem. Biophys. Methods 35 (1997) 115-128. (Pubitemid 27414542)
    • (1997) Journal of Biochemical and Biophysical Methods , vol.35 , Issue.2 , pp. 115-128
    • Khramtsov, V.V.1    Yelinova, V.I.2    Glazachev, Yu.I.3    Reznikov, V.A.4    Zimmer, G.5
  • 54
    • 84857498912 scopus 로고    scopus 로고
    • Protein design using continuous rotamers
    • P. Gainza, K.E. Roberts, B.R. Donald, Protein design using continuous rotamers, PLoS Comput. Biol. (2012), http://dx.doi.org/10.1371/journal.pcbi. 1002335.
    • (2012) PLoS Comput. Biol. , pp. 1002335
    • Gainza, P.1    Roberts, K.E.2    Donald, B.R.3
  • 56
    • 0025047629 scopus 로고
    • A mutant T4 Lysozyme displays five different crystal conformations
    • H.R. Faber, B.W. Matthews, A mutant T4 Lysozyme displays five different crystal conformations, Nature 348 (1990) 263-266.
    • (1990) Nature , vol.348 , pp. 263-266
    • Faber, H.R.1    Matthews, B.W.2
  • 57
    • 77952099112 scopus 로고    scopus 로고
    • Distance and dynamics determination by W-band DEER and W-band ST-EPR
    • L. Song, M. Larion, J. Chamoun, M. Bonora, P.G. Fajer, Distance and dynamics determination by W-band DEER and W-band ST-EPR, Eur. Biophys. J. 39 (2010) 711-719.
    • (2010) Eur. Biophys. J. , vol.39 , pp. 711-719
    • Song, L.1    Larion, M.2    Chamoun, J.3    Bonora, M.4    Fajer, P.G.5
  • 58
    • 79251562868 scopus 로고    scopus 로고
    • Rotamer libraries of spin-labelled cysteins for protein studies
    • Y. Polyhach, E. Bordignon, G. Jeschke, Rotamer libraries of spin-labelled cysteins for protein studies, PCCP 13 (2011) 2356-2366.
    • (2011) PCCP , vol.13 , pp. 2356-2366
    • Polyhach, Y.1    Bordignon, E.2    Jeschke, G.3
  • 59
    • 44349127313 scopus 로고    scopus 로고
    • Using quantum mechanics to improve estimates of amino acid side chain rotamer energies
    • DOI 10.1002/prot.21845
    • P.D. Renfrew, G. Butterfoss, B. Kuhlman, Using quantum mechanics to improve estimates of amino acid side chain rotamer energies, Proteins 71 (2008) 1637- 1646. (Pubitemid 351732923)
    • (2008) Proteins: Structure, Function and Genetics , vol.71 , Issue.4 , pp. 1637-1646
    • Renfrew, P.D.1    Butterfoss, G.L.2    Kuhlman, B.3
  • 60
    • 3242801220 scopus 로고    scopus 로고
    • Site-directed electrostatic measurements with a thiol-specific pH-sensitive nitroxide: Differentiating local pK and polarity effects by high-field EPR
    • DOI 10.1021/ja048801f
    • P.I. Smirnov, A. Ruuge, V.A. Reznikov, M.A. Voinov, I.A. Grigorev, Site-directed electrostatic measurements with a thiol-specific pH-sensitive nitroxide: differentiating local pK and polarity effects by high-field EPR, J. Am. Chem. Soc. 126 (2004) 8872-8873. (Pubitemid 38971042)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.29 , pp. 8872-8873
    • Smirnov, A.I.1    Ruuge, A.2    Reznikov, V.A.3    Voinov, M.A.4    Grigor'Ev, I.A.5


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