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Volumn 64, Issue , 2013, Pages 507-532

Dynamic nuclear polarization methods in solids and solutions to explore membrane proteins and membrane systems

Author keywords

Electron paramagnetic resonance; GPCRs; Hydration dynamics; Lipid protein interactions; Magic angle spinning; Structural determination

Indexed keywords

CYTOLOGY; DYNAMICS; HYDRATION; LIPIDS; MAGIC ANGLE SPINNING; PARAMAGNETIC RESONANCE; PARAMAGNETISM; PROTEINS;

EID: 84875993174     PISSN: 0066426X     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev-physchem-040412-110028     Document Type: Article
Times cited : (38)

References (152)
  • 1
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin E, von Heijne G. 1998. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci. 7:1029-38
    • (1998) Protein Sci. , vol.7 , pp. 1029-1038
    • Wallin, E.1    Von Heijne, G.2
  • 2
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson CM. 2006. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75:333-66
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 4
    • 79551597049 scopus 로고    scopus 로고
    • Influence of solubilizing environments on membrane protein structures
    • Cross TA, Sharma M, Yi M, Zhou HX. 2011. Influence of solubilizing environments on membrane protein structures. Trends Biochem. Sci. 36:117-25
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 117-125
    • Cross, T.A.1    Sharma, M.2    Yi, M.3    Zhou, H.X.4
  • 5
    • 49749095639 scopus 로고    scopus 로고
    • Lipids and membrane protein structures
    • Hunte C, Richers S. 2008. Lipids and membrane protein structures. Curr. Opin. Struct. Biol. 18:406-11
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 406-411
    • Hunte, C.1    Richers, S.2
  • 6
    • 48249095616 scopus 로고    scopus 로고
    • How translocons select transmembrane helices
    • White SH, von Heijne G. 2008. How translocons select transmembrane helices. Annu. Rev. Biophys. 37:23-42
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 23-42
    • White, S.H.1    Von Heijne, G.2
  • 7
    • 82355173188 scopus 로고    scopus 로고
    • Hydrophobicity scales: A thermodynamic looking glass into lipid-protein interactions
    • MacCallum JL, Tieleman DP. 2011. Hydrophobicity scales: A thermodynamic looking glass into lipid-protein interactions. Trends Biochem. Sci. 36:653-62
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 653-662
    • Maccallum, J.L.1    Tieleman, D.P.2
  • 8
    • 34247844535 scopus 로고    scopus 로고
    • Direct imaging of individual intrinsic hydration layers on lipid bilayers at Angstrom resolution
    • Fukuma T, Higgins MJ, Jarvis SP. 2007. Direct imaging of individual intrinsic hydration layers on lipid bilayers at Angstrom resolution. Biophys. J. 92:3603-9
    • (2007) Biophys. J. , vol.92 , pp. 3603-3609
    • Fukuma, T.1    Higgins, M.J.2    Jarvis, S.P.3
  • 9
    • 0024346677 scopus 로고
    • Hydrophobic organization of membrane proteins
    • Rees DC, DeAntonio L, Eisenberg D. 1989. Hydrophobic organization of membrane proteins. Science 245:510-13
    • (1989) Science , vol.245 , pp. 510-513
    • Rees, D.C.1    Deantonio, L.2    Eisenberg, D.3
  • 10
    • 66249083118 scopus 로고    scopus 로고
    • Emerging roles for lipids in shaping membrane-protein function
    • Phillips R, Ursell T,Wiggins P, Sens P. 2009. Emerging roles for lipids in shaping membrane-protein function. Nature 459:379-85
    • (2009) Nature , vol.459 , pp. 379-385
    • Phillips, R.1    Ursell Twiggins, P.2    Sens, P.3
  • 11
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood D, Simons K. 2010. Lipid rafts as a membrane-organizing principle. Science 327:46-50
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 12
    • 84861675099 scopus 로고    scopus 로고
    • The amyloid precursor protein has a flexible transmembrane domain and binds cholesterol
    • Barrett PJ, Song J, Van Horn WD, Hustedt EJ, Schafer JM, et al. 2012. The amyloid precursor protein has a flexible transmembrane domain and binds cholesterol. Science 336:1168-71
    • (2012) Science , vol.336 , pp. 1168-1171
    • Barrett, P.J.1    Song, J.2    Van Horn, W.D.3    Hustedt, E.J.4    Schafer, J.M.5
  • 13
    • 77952934647 scopus 로고    scopus 로고
    • Lipids and cholesterol as regulators of traffic in the endomembrane system
    • Lippincott-Schwartz J, Phair RD. 2010. Lipids and cholesterol as regulators of traffic in the endomembrane system. Annu. Rev. Biophys. 39:559-78
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 559-578
    • Lippincott-Schwartz, J.1    Phair, R.D.2
  • 14
    • 84857650478 scopus 로고    scopus 로고
    • Hydrogen bond dynamics in membrane protein function
    • Bondar AN,White SH. 2012. Hydrogen bond dynamics in membrane protein function. Biochim. Biophys. Acta 1818:942-50
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 942-950
    • Bondar, A.N.1    White, S.H.2
  • 15
    • 2142715470 scopus 로고    scopus 로고
    • Water dynamics and dewetting transitions in the small mechanosensitive channel MscS
    • Anishkin A, Sukharev S. 2004. Water dynamics and dewetting transitions in the small mechanosensitive channel MscS. Biophys. J. 86:2883-95
    • (2004) Biophys. J. , vol.86 , pp. 2883-2895
    • Anishkin, A.1    Sukharev, S.2
  • 16
    • 44049105071 scopus 로고    scopus 로고
    • Cell water dynamics on multiple time scales
    • Persson E, Halle B. 2008. Cell water dynamics on multiple time scales. Proc. Natl. Acad. Sci. USA 105:6266-71
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 6266-6271
    • Persson, E.1    Halle, B.2
  • 17
    • 66649096395 scopus 로고    scopus 로고
    • Conserved waters mediate structural and functional activation of family A (rhodopsin-like) G protein-coupled receptors
    • Angel TE, Chance MR, Palczewski K. 2009. Conserved waters mediate structural and functional activation of family A (rhodopsin-like) G protein-coupled receptors. Proc. Natl. Acad. Sci. USA 106:8555-60
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 8555-8560
    • Angel, T.E.1    Chance, M.R.2    Palczewski, K.3
  • 18
    • 79960979207 scopus 로고    scopus 로고
    • Proton transfer via a transient linear water-molecule chain in a membrane protein
    • Freier E, Wolf S, Gerwert K. 2011. Proton transfer via a transient linear water-molecule chain in a membrane protein. Proc. Natl. Acad. Sci. USA 108:11435-39
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 11435-11439
    • Freier, E.1    Wolf, S.2    Gerwert, K.3
  • 19
    • 0036661083 scopus 로고    scopus 로고
    • Aquaporin water channels: From atomic structure to clinical medicine
    • Agre P, King LS, Yasui M, Guggino WB, Ottersen OP, et al. 2002. Aquaporin water channels: from atomic structure to clinical medicine. J. Physiol. 542:3-16
    • (2002) J. Physiol. , vol.542 , pp. 3-16
    • Agre, P.1    King, L.S.2    Yasui, M.3    Guggino, W.B.4    Ottersen, O.P.5
  • 20
    • 80054967217 scopus 로고    scopus 로고
    • Correlated structural kinetics and retarded solvent dynamics at the metalloprotease active site
    • Grossman M, Born B, Heyden M, Tworowski D, Fields GB, et al. 2011. Correlated structural kinetics and retarded solvent dynamics at the metalloprotease active site. Nat. Struct. Mol. Biol. 18:1102-8
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 1102-1108
    • Grossman, M.1    Born, B.2    Heyden, M.3    Tworowski, D.4    Fields, G.B.5
  • 21
    • 38949183943 scopus 로고    scopus 로고
    • Nanosecond to microsecond protein dynamics probed by magnetic relaxation dispersion of buried water molecules
    • Persson E, Halle B. 2008. Nanosecond to microsecond protein dynamics probed by magnetic relaxation dispersion of buried water molecules. J. Am. Chem. Soc. 130:1774-87
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 1774-1787
    • Persson, E.1    Halle, B.2
  • 22
    • 79954497065 scopus 로고    scopus 로고
    • Site-specific hydration dynamics in the nonpolar core of a molten globule by dynamic nuclear polarization of water
    • Armstrong BD, Choi J, Lopez C,Wesener DA, Hubbell W, et al. 2011. Site-specific hydration dynamics in the nonpolar core of a molten globule by dynamic nuclear polarization of water. J. Am. Chem. Soc. 133:5987-95
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 5987-5995
    • Armstrong, B.D.1    Choi, J.2    Lopez Cwesener, D.A.3    Hubbell, W.4
  • 23
    • 79551637126 scopus 로고    scopus 로고
    • Site-resolved measurement of water-protein interactions by solution NMR
    • Nucci NV, Pometun MS,Wand AJ. 2011. Site-resolved measurement of water-protein interactions by solution NMR. Nat. Struct. Mol. Biol. 18:245-49
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 245-249
    • Nucci, N.V.1    Pometun, M.S.2    Wand, A.J.3
  • 24
    • 68049087927 scopus 로고    scopus 로고
    • Protein hydration dynamics and molecular mechanism of coupled water-protein fluctuations
    • Zhang LY, Yang Y, Kao YT, Wang LJ, Zhong DP. 2009. Protein hydration dynamics and molecular mechanism of coupled water-protein fluctuations. J. Am. Chem. Soc. 131:10677-91
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 10677-10691
    • Zhang, L.Y.1    Yang, Y.2    Kao, Y.T.3    Wang, L.J.4    Zhong, D.P.5
  • 25
    • 0037133342 scopus 로고    scopus 로고
    • Biological water at the protein surface: Dynamical solvation probed directly with femtosecond resolution
    • Pal SK, Peon J, Zewail AH. 2002. Biological water at the protein surface: dynamical solvation probed directly with femtosecond resolution. Proc. Natl. Acad. Sci. USA 99:1763-68
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1763-1768
    • Pal, S.K.1    Peon, J.2    Zewail, A.H.3
  • 26
    • 1542375172 scopus 로고    scopus 로고
    • Hydration dynamics near a model protein surface
    • Russo D, Hura G, Head-Gordon T. 2004. Hydration dynamics near a model protein surface. Biophys. J. 86:1852-62
    • (2004) Biophys. J. , vol.86 , pp. 1852-1862
    • Russo, D.1    Hura, G.2    Head-Gordon, T.3
  • 27
    • 26944481188 scopus 로고    scopus 로고
    • Interfaces and the driving force of hydrophobic assembly
    • Chandler D.
    • Chandler D. 2005. Interfaces and the driving force of hydrophobic assembly. Nature 437:640-47
    • (2005) Nature , vol.437 , pp. 640-647
  • 28
    • 34547485422 scopus 로고    scopus 로고
    • How protein surfaces induce anomalous dynamics of hydration water
    • Pizzitutti F, Marchi M, Sterpone F, Rossky PJ. 2007. How protein surfaces induce anomalous dynamics of hydration water. J. Phys. Chem. B 111:7584-90
    • (2007) J. Phys. Chem. B , vol.111 , pp. 7584-7590
    • Pizzitutti, F.1    Marchi, M.2    Sterpone, F.3    Rossky, P.J.4
  • 33
    • 0037391107 scopus 로고    scopus 로고
    • Membrane protein crystallization
    • Caffrey M. 2003. Membrane protein crystallization. J. Struct. Biol. 142:108-32
    • (2003) J. Struct. Biol. , vol.142 , pp. 108-132
    • Caffrey, M.1
  • 34
    • 0343777458 scopus 로고    scopus 로고
    • Observing single biomolecules at work with the atomic force microscope
    • Engel A, Muller DJ. 2000. Observing single biomolecules at work with the atomic force microscope. Nat. Struct. Biol. 7:715-18
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 715-718
    • Engel, A.1    Muller, D.J.2
  • 35
    • 34249894142 scopus 로고    scopus 로고
    • Small-angle X-ray scattering from RNA, proteins, and protein complexes
    • Lipfert J, Doniach S. 2007. Small-angle X-ray scattering from RNA, proteins, and protein complexes. Annu. Rev. Biophys. Biomol. Struct. 36:307-27
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36 , pp. 307-327
    • Lipfert, J.1    Doniach, S.2
  • 36
    • 0242574743 scopus 로고    scopus 로고
    • Visualization ofmembrane protein domains by cryo-electron microscopy of dengue virus
    • ZhangW, Chipman PR, Corver J, Johnson PR, Zhang Y, et al. 2003. Visualization ofmembrane protein domains by cryo-electron microscopy of dengue virus. Nat. Struct. Biol. 10:907-12
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 907-912
    • Zhang, W.1    Chipman, P.R.2    Corver, J.3    Johnson, P.R.4    Zhang, Y.5
  • 37
    • 40949163372 scopus 로고    scopus 로고
    • Distance measurements in the borderline region of applicability of CW EPR and DEER: A model study on a homologous series of spin-labelled peptides
    • Banham JE, BakerCM, Ceola S,Day IJ, GrantGH, et al. 2008. Distance measurements in the borderline region of applicability of CW EPR and DEER: A model study on a homologous series of spin-labelled peptides. J. Magn. Reson. 191:202-18
    • (2008) J. Magn. Reson. , vol.191 , pp. 202-218
    • Banham, J.E.1    Baker, C.M.2    Ceola, S.3    Day, I.J.4    Grant, G.H.5
  • 38
    • 0009924593 scopus 로고    scopus 로고
    • Double-quantum ESR and distance measurements
    • ed. LJ Berliner, GR Eaton, SS Eaton New York: Springer
    • Borbat P, Freed J. 2002. Double-quantum ESR and distance measurements. In Distance Measurements in Biological Systems by EPR, ed. LJ Berliner, GR Eaton, SS Eaton, pp. 383-459. New York: Springer
    • (2002) Distance Measurements in Biological Systems by EPR , pp. 383-459
    • Borbat, P.1    Freed, J.2
  • 39
    • 0034132251 scopus 로고    scopus 로고
    • Dead-time free measurement of dipole-dipole interactions between electron spins
    • Pannier M, Veit S, Godt A, Jeschke G, Spiess HW. 2000. Dead-time free measurement of dipole-dipole interactions between electron spins. J. Magn. Reson. 142:331-40
    • (2000) J. Magn. Reson. , vol.142 , pp. 331-340
    • Pannier, M.1    Veit, S.2    Godt, A.3    Jeschke, G.4    Spiess, H.W.5
  • 40
    • 0029115328 scopus 로고
    • Determination of the distance between two spin labels attached to a macromolecule
    • Rabenstein MD, Shin YK. 1995. Determination of the distance between two spin labels attached to a macromolecule. Proc. Natl. Acad. Sci. USA 92:8239-43
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8239-8243
    • Rabenstein, M.D.1    Shin, Y.K.2
  • 41
    • 0030781782 scopus 로고    scopus 로고
    • Determination of interspin distances between spin labels attached to insulin: Comparison of electron paramagnetic resonance data with the X-ray structure
    • Steinhoff HJ, Radzwill N, Thevis W, Lenz V, Brandenburg D, et al. 1997. Determination of interspin distances between spin labels attached to insulin: comparison of electron paramagnetic resonance data with the X-ray structure. Biophys. J. 73:3287-98
    • (1997) Biophys. J. , vol.73 , pp. 3287-3298
    • Steinhoff, H.J.1    Radzwill, N.2    Thevis, W.3    Lenz, V.4    Brandenburg, D.5
  • 43
    • 67749091066 scopus 로고    scopus 로고
    • Multifrequency electron spin resonance spectra of a spin-labeled protein calculated from molecular dynamics simulations
    • Sezer D, Freed JH, Roux B. 2009. Multifrequency electron spin resonance spectra of a spin-labeled protein calculated from molecular dynamics simulations. J. Am. Chem. Soc. 131:2597-605
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 2597-2605
    • Sezer, D.1    Freed, J.H.2    Roux, B.3
  • 44
    • 0028346566 scopus 로고
    • A collision gradient method to determine the immersion depth of nitroxides in lipid bilayers: Application to spin-labeled mutants of bacteriorhodopsin
    • Altenbach C, Greenhalgh DA, Khorana HG, Hubbell WL. 1994. 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 91:1667-71
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1667-1671
    • Altenbach, C.1    Greenhalgh, D.A.2    Khorana, H.G.3    Hubbell, W.L.4
  • 45
    • 0037150098 scopus 로고    scopus 로고
    • Membrane orientation and position of the C2 domain from cPLA2 by site-directed spin labeling
    • Frazier AA, Wisner MA,Malmberg NJ, Victor KG, Fanucci GE, et al. 2002. Membrane orientation and position of the C2 domain from cPLA2 by site-directed spin labeling. Biochemistry 41:6282-92
    • (2002) Biochemistry , vol.41 , pp. 6282-6292
    • Frazier, A.A.1    Wisner, M.A.2    Malmberg, N.J.3    Victor, K.G.4    Fanucci, G.E.5
  • 46
    • 34548702230 scopus 로고    scopus 로고
    • A new model for Overhauser enhanced nuclear magnetic resonance using nitroxide radicals
    • Armstrong BD, Han S. 2007. A new model for Overhauser enhanced nuclear magnetic resonance using nitroxide radicals. J. Chem. Phys. 127:104508
    • (2007) J. Chem. Phys. , vol.127 , pp. 104508
    • Armstrong, B.D.1    Han, S.2
  • 47
    • 67949118702 scopus 로고    scopus 로고
    • Overhauser dynamic nuclear polarization to study local water dynamics
    • Armstrong BD, Han S. 2009. Overhauser dynamic nuclear polarization to study local water dynamics. J. Am. Chem. Soc. 131:4641-47
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 4641-4647
    • Armstrong, B.D.1    Han, S.2
  • 49
    • 0242377687 scopus 로고
    • NMR relaxation dispersion in an aqueous nitroxide system
    • Borah B, Bryant RG. 1981. NMR relaxation dispersion in an aqueous nitroxide system. J. Chem. Phys. 75:3297-300
    • (1981) J. Chem. Phys. , vol.75 , pp. 3297-3300
    • Borah, B.1    Bryant, R.G.2
  • 51
    • 84859912916 scopus 로고    scopus 로고
    • Membrane protein structure and dynamics from NMR spectroscopy
    • Hong M, Zhang Y, Hu F. 2012. Membrane protein structure and dynamics from NMR spectroscopy. Annu. Rev. Phys. Chem. 63:1-24
    • (2012) Annu. Rev. Phys. Chem. , vol.63 , pp. 1-24
    • Hong, M.1    Zhang, Y.2    Hu, F.3
  • 52
    • 67650285019 scopus 로고    scopus 로고
    • Structure and dynamics of membrane proteins by magic angle spinning solid-state NMR
    • McDermott A. 2009. Structure and dynamics of membrane proteins by magic angle spinning solid-state NMR. Annu. Rev. Biophys. 38:385-403
    • (2009) Annu. Rev. Biophys. , vol.38 , pp. 385-403
    • McDermott, A.1
  • 53
    • 77952896921 scopus 로고    scopus 로고
    • High field dynamic nuclear polarization: The renaissance
    • Griffin RG, Prisner TF. 2010. High field dynamic nuclear polarization: The renaissance. Phys. Chem. Chem. Phys. 12:5737-40
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 5737-5740
    • Griffin, R.G.1    Prisner, T.F.2
  • 54
    • 77952934340 scopus 로고    scopus 로고
    • Solid-state dynamic nuclear polarization at 263 GHz: Spectrometer design and experimental results
    • Rosay M, Tometich L, Pawsey S, Bader R, Schauwecker R, et al. 2010. Solid-state dynamic nuclear polarization at 263 GHz: spectrometer design and experimental results. Phys. Chem. Chem. Phys. 12:5850- 60
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 5850-5860
    • Rosay, M.1    Tometich, L.2    Pawsey, S.3    Bader, R.4    Schauwecker, R.5
  • 55
    • 79953293753 scopus 로고    scopus 로고
    • Quantum mechanical theory of dynamic nuclear polarization in solid dielectrics
    • Hu KN, Debelouchina GT, Smith AA, Griffin RG. 2011. Quantum mechanical theory of dynamic nuclear polarization in solid dielectrics. J. Chem. Phys. 134:125105
    • (2011) J. Chem. Phys. , vol.134 , pp. 125105
    • Hu, K.N.1    Debelouchina, G.T.2    Smith, A.A.3    Griffin, R.G.4
  • 56
    • 84859355671 scopus 로고    scopus 로고
    • Dynamic nuclear polarization in the solid state: A transition between the cross effect and the solid effect
    • Shimon D, Hovav Y, Feintuch A, Goldfarb D, Vega S. 2012. Dynamic nuclear polarization in the solid state: A transition between the cross effect and the solid effect. Phys. Chem. Chem. Phys. 14:5729-43
    • (2012) Phys. Chem. Chem. Phys. , vol.14 , pp. 5729-5743
    • Shimon, D.1    Hovav, Y.2    Feintuch, A.3    Goldfarb, D.4    Vega, S.5
  • 59
    • 0037824712 scopus 로고    scopus 로고
    • Dynamic nuclear polarization at 9T using a novel 250 GHz gyrotron microwave source
    • Bajaj VS, Farrar CT, Mastovsky I, Vieregg J, Bryant J, et al. 2003. Dynamic nuclear polarization at 9T using a novel 250 GHz gyrotron microwave source. J. Magn. Reson. 160:85-90
    • (2003) J. Magn. Reson. , vol.160 , pp. 85-90
    • Bajaj, V.S.1    Farrar, C.T.2    Mastovsky, I.3    Vieregg, J.4    Bryant, J.5
  • 60
    • 35748961102 scopus 로고    scopus 로고
    • 250 GHz CW gyrotron oscillator for dynamic nuclear polarization in biological solid state NMR
    • Bajaj VS, Hornstein MK, Kreischer KE, Sirigiri JR, Woskov PP, et al. 2007. 250 GHz CW gyrotron oscillator for dynamic nuclear polarization in biological solid state NMR. J. Magn. Reson. 189:251-79
    • (2007) J. Magn. Reson. , vol.189 , pp. 251-279
    • Bajaj, V.S.1    Hornstein, M.K.2    Kreischer, K.E.3    Sirigiri, J.R.4    Woskov, P.P.5
  • 61
    • 77953307773 scopus 로고    scopus 로고
    • Continuous-wave operation of a frequency-tunable 460-GHz second-harmonic gyrotron for enhanced nuclear magnetic resonance
    • Torrezan AC, Han ST, Mastovsky I, Shapiro MA, Sirigiri JR, et al. 2010. Continuous-wave operation of a frequency-tunable 460-GHz second-harmonic gyrotron for enhanced nuclear magnetic resonance. IEEE Trans. Plasma Sci. 38:1150-60
    • (2010) IEEE Trans. Plasma Sci. , vol.38 , pp. 1150-1160
    • Torrezan, A.C.1    Han, S.T.2    Mastovsky, I.3    Shapiro, M.A.4    Sirigiri, J.R.5
  • 63
    • 84855659020 scopus 로고    scopus 로고
    • A multi-sample 94 GHz dissolution dynamic-nuclear-polarization system
    • Batel M, Krajewski M, Weiss K, With O, Dapp A, et al. 2012. A multi-sample 94 GHz dissolution dynamic-nuclear-polarization system. J. Magn. Reson. 214:166-74
    • (2012) J. Magn. Reson. , vol.214 , pp. 166-174
    • Batel, M.1    Krajewski, M.2    Weiss, K.3    With, O.4    Dapp, A.5
  • 65
    • 79951821785 scopus 로고    scopus 로고
    • Fast characterization of functionalized silica materials by silicon-29 surface-enhanced NMR spectroscopy using dynamic nuclear polarization
    • Lelli M, GajanD,LesageA,CaporiniMA, VitzthumV, et al. 2011. Fast characterization of functionalized silica materials by silicon-29 surface-enhanced NMR spectroscopy using dynamic nuclear polarization. J. Am. Chem. Soc. 133:2104-7
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 2104-2107
    • Lelli, M.1    Gajan, D.2    Lesage, A.3    Caporini, M.A.4    Vitzthumv5
  • 66
    • 77952894535 scopus 로고    scopus 로고
    • Dynamic nuclear polarization-enhanced solid-state NMR spectroscopy of GNNQQNY nanocrystals and amyloid fibrils
    • Debelouchina GT, Bayro MJ, van derWel PCA, CaporiniMA, Barnes AB, et al. 2010. Dynamic nuclear polarization-enhanced solid-state NMR spectroscopy of GNNQQNY nanocrystals and amyloid fibrils. Phys. Chem. Chem. Phys. 12:5911-19
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 5911-5919
    • Debelouchina, G.T.1    Bayro, M.J.2    Van Derwel, P.C.A.3    Caporini, M.A.4    Barnes, A.B.5
  • 67
    • 80052335544 scopus 로고    scopus 로고
    • Intermolecular structure determination of amyloid fibrils with magic-angle spinning and dynamic nuclear polarization NMR
    • BayroMJ, Debelouchina GT, Eddy MT, Birkett NR,MacPheeCE, et al. 2011. Intermolecular structure determination of amyloid fibrils with magic-angle spinning and dynamic nuclear polarization NMR. J. Am. Chem. Soc. 133:13967-74
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 13967-13974
    • Bayro, M.J.1    Debelouchina, G.T.2    Eddy, M.T.3    Birkett, N.R.4    Macphee, C.E.5
  • 70
    • 77952948686 scopus 로고    scopus 로고
    • Prospects for sub-micron solid state nuclear magnetic resonance imaging with low-temperature dynamic nuclear polarization
    • Thurber KR, Tycko R. 2010. Prospects for sub-micron solid state nuclear magnetic resonance imaging with low-temperature dynamic nuclear polarization. Phys. Chem. Chem. Phys. 12:5779-85
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 5779-5785
    • Thurber, K.R.1    Tycko, R.2
  • 71
    • 77955228127 scopus 로고    scopus 로고
    • Low-temperature dynamic nuclear polarization at 9.4 T with a 30 mW microwave source
    • Thurber KR, YauWM, Tycko R. 2010. Low-temperature dynamic nuclear polarization at 9.4 T with a 30 mW microwave source. J. Magn. Reson. 204:303-13
    • (2010) J. Magn. Reson. , vol.204 , pp. 303-313
    • Thurber, K.R.1    Yau, W.M.2    Tycko, R.3
  • 72
    • 84864193798 scopus 로고    scopus 로고
    • Inductively coupled NMR probe for versatile dynamic nuclear polarization operation at 7 Tesla: Observation of 61 ?2% 1H polarization at 4 K
    • Siawa TA, Walkera SA, Armstrong BD, Han S. 2012. Inductively coupled NMR probe for versatile dynamic nuclear polarization operation at 7 Tesla: observation of 61 ?2% 1H polarization at 4 K. J. Magn. Reson. 221:5-10
    • (2012) J. Magn. Reson. , vol.221 , pp. 5-10
    • Siawa, T.A.1    Walkera, S.A.2    Armstrong, B.D.3    Han, S.4
  • 73
    • 80052605560 scopus 로고    scopus 로고
    • Polarizing agents and mechanisms for high-field dynamic nuclear polarization of frozen dielectric solids
    • Hu KN. 2011. Polarizing agents and mechanisms for high-field dynamic nuclear polarization of frozen dielectric solids. Solid State Nucl. Magn. Reson. 40:31-41
    • (2011) Solid State Nucl. Magn. Reson. , vol.40 , pp. 31-41
    • Hu, K.N.1
  • 75
    • 42949177561 scopus 로고    scopus 로고
    • High-frequency dynamic nuclear polarization using biradicals: A multifrequency EPR lineshape analysis
    • Hu KN, Song C, Yu HH, Swager TM, Griffin RG. 2008. High-frequency dynamic nuclear polarization using biradicals: A multifrequency EPR lineshape analysis. J. Chem. Phys. 128:052302
    • (2008) J. Chem. Phys. , vol.128 , pp. 052302
    • Hu, K.N.1    Song, C.2    Yu, H.H.3    Swager, T.M.4    Griffin, R.G.5
  • 76
    • 33748353607 scopus 로고    scopus 로고
    • TOTAPOL: A biradical polarizing agent for dynamic nuclear polarization experiments in aqueous media
    • Song CS, Hu KN, Joo CG, Swager TM, Griffin RG. 2006. TOTAPOL: A biradical polarizing agent for dynamic nuclear polarization experiments in aqueous media. J. Am. Chem. Soc. 128:11385-90
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 11385-11390
    • Song, C.S.1    Hu, K.N.2    Joo, C.G.3    Swager, T.M.4    Griffin, R.G.5
  • 78
    • 84856444127 scopus 로고    scopus 로고
    • A slowly relaxing rigid biradical for efficient dynamic nuclear polarization surface-enhanced NMR spectroscopy: Expeditious characterization of functional group manipulation in hybrid materials
    • Zagdoun A, Casano G, Ouari O, Lapadula G, Rossini AJ, et al. 2012. A slowly relaxing rigid biradical for efficient dynamic nuclear polarization surface-enhanced NMR spectroscopy: expeditious characterization of functional group manipulation in hybrid materials. J. Am. Chem. Soc. 134:2284-91
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 2284-2291
    • Zagdoun, A.1    Casano, G.2    Ouari, O.3    Lapadula, G.4    Rossini, A.J.5
  • 80
    • 84856444127 scopus 로고    scopus 로고
    • A slowly relaxing rigid biradical for efficient dynamic nuclear polarization surface-enhanced NMR spectroscopy: Expeditious characterization of functional group manipulation in hybrid materials
    • Zagdoun A, Casano G, Ouari O, Lapadula G, Rossini AJ, et al. 2012. A slowly relaxing rigid biradical for efficient dynamic nuclear polarization surface-enhanced NMR spectroscopy: expeditious characterization of functional group manipulation in hybrid materials. J. Am. Chem. Soc. 134:2284-91
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 2284-2291
    • Zagdoun, A.1    Casano, G.2    Ouari, O.3    Lapadula, G.4    Rossini, A.J.5
  • 81
    • 67249096746 scopus 로고    scopus 로고
    • Functional and shunt states of bacteriorhodopsin resolved by 250 GHz dynamic nuclear polarization-enhanced solidstate NMR
    • Bajaj VS, Mak-Jurkauskas ML, Belenky M, Herzfeld J, Griffin RG. 2009. Functional and shunt states of bacteriorhodopsin resolved by 250 GHz dynamic nuclear polarization-enhanced solidstate NMR. Proc. Natl. Acad. Sci. USA 106:9244-49
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 9244-9249
    • Bajaj, V.S.1    Mak-Jurkauskas, M.L.2    Belenky, M.3    Herzfeld, J.4    Griffin, R.G.5
  • 83
    • 81855172000 scopus 로고    scopus 로고
    • Dynamic nuclear polarization-enhanced solid-state NMR of a 13C-labeled signal peptide bound to lipid-reconstituted SecYEG translocon
    • Reggie L, Lopez JJ, Collinson I, Glaubitz C, Lorch M. 2011. Dynamic nuclear polarization-enhanced solid-state NMR of a 13C-labeled signal peptide bound to lipid-reconstituted SecYEG translocon. J. Am. Chem. Soc. 133:19084-86
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 19084-19086
    • Reggie, L.1    Lopez, J.J.2    Collinson, I.3    Glaubitz, C.4    Lorch, M.5
  • 84
    • 84855419218 scopus 로고    scopus 로고
    • Characterization of membrane proteins in isolated native cellular membranes by dynamic nuclear polarization solid-state NMR spectroscopy without purification and reconstitution
    • Jacso T, Franks WT, Rose H, Fink U, Broecker J, et al. 2012. Characterization of membrane proteins in isolated native cellular membranes by dynamic nuclear polarization solid-state NMR spectroscopy without purification and reconstitution. Angew. Chem. Int. Ed. Engl. 51:432-35
    • (2012) Angew. Chem. Int. Ed. Engl. , vol.51 , pp. 432-435
    • Jacso, T.1    Franks, W.T.2    Rose, H.3    Fink, U.4    Broecker, J.5
  • 85
    • 77951692765 scopus 로고    scopus 로고
    • Solid-state NMR spectroscopy of oriented membrane polypeptides at 100 K with signal enhancement by dynamic nuclear polarization
    • Salnikov E, Rosay M, Pawsey S, Ouari O, Tordo P, Bechinger B. 2010. Solid-state NMR spectroscopy of oriented membrane polypeptides at 100 K with signal enhancement by dynamic nuclear polarization. J. Am. Chem. Soc. 132:5940-41
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 5940-5941
    • Salnikov, E.1    Rosay, M.2    Pawsey, S.3    Ouari, O.4    Tordo, P.5    Bechinger, B.6
  • 87
    • 84858275751 scopus 로고    scopus 로고
    • Solid-state NMR spectroscopy on cellular preparations enhanced by dynamic nuclear polarization
    • Renault M, Pawsey S, Bos MP, Koers EJ, Nand D, et al. 2012. Solid-state NMR spectroscopy on cellular preparations enhanced by dynamic nuclear polarization. Angew. Chem. Int. Ed. Engl. 51:2998-3001
    • (2012) Angew. Chem. Int. Ed. Engl. , vol.51 , pp. 2998-3001
    • Renault, M.1    Pawsey, S.2    Bos, M.P.3    Koers, E.J.4    Nand, D.5
  • 88
    • 84858332807 scopus 로고    scopus 로고
    • The effect of biradical concentration on the performance of DNP-MAS-NMR
    • Lange S, Linden AH, Akbey U, Franks WT, Loening NM, et al. 2012. The effect of biradical concentration on the performance of DNP-MAS-NMR. J. Magn. Reson. 216:209-12
    • (2012) J. Magn. Reson. , vol.216 , pp. 209-212
    • Lange, S.1    Linden, A.H.2    Akbey, U.3    Franks, W.T.4    Loening, N.M.5
  • 89
    • 0027110802 scopus 로고
    • Mechanism of DNP-enhanced polarization transfer across the interface of polycarbonate polystyrene heterogeneous blends
    • Afeworki M, Schaefer J. 1992. Mechanism of DNP-enhanced polarization transfer across the interface of polycarbonate polystyrene heterogeneous blends. Macromolecules 25:4092-96
    • (1992) Macromolecules , vol.25 , pp. 4092-4096
    • Afeworki, M.1    Schaefer, J.2
  • 90
    • 59849124612 scopus 로고    scopus 로고
    • Dynamic nuclear polarization and spin diffusion in nonconducting solids
    • Ramanathan C. 2008. Dynamic nuclear polarization and spin diffusion in nonconducting solids. Appl. Magn. Reson. 34:409-21
    • (2008) Appl. Magn. Reson. , vol.34 , pp. 409-421
    • Ramanathan, C.1
  • 91
    • 33747799315 scopus 로고    scopus 로고
    • Dynamic nuclear polarization of amyloidogenic peptide nanocrystals:GNNQQNY, a core segment of the yeast prion protein Sup35p
    • van der Wel PCA, Hu KN, Lewandowski J, Griffin RG. 2006. Dynamic nuclear polarization of amyloidogenic peptide nanocrystals:GNNQQNY, a core segment of the yeast prion protein Sup35p. J. Am. Chem. Soc. 128:10840-46
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 10840-10846
    • Van Der Wel Pca1    Hu, K.N.2    Lewandowski, J.3    Griffin, R.G.4
  • 92
    • 0030939741 scopus 로고    scopus 로고
    • Polarization-enhanced NMR spectroscopy of biomolecules in frozen solution
    • Hall DA, Maus DC, Gerfen GJ, Inati SJ, Becerra LR, et al. 1997. Polarization-enhanced NMR spectroscopy of biomolecules in frozen solution. Science 276:930-32
    • (1997) Science , vol.276 , pp. 930-932
    • Hall, D.A.1    Maus, D.C.2    Gerfen, G.J.3    Inati, S.J.4    Becerra, L.R.5
  • 93
    • 0035819628 scopus 로고    scopus 로고
    • Sensitivity-enhanced NMR of biological solids: Dynamic nuclear polarization of Y21M fd bacteriophage and purple membrane
    • Rosay M, Zeri AC, Astrof NS, Opella SJ, Herzfeld J, Griffin RG. 2001. Sensitivity-enhanced NMR of biological solids: dynamic nuclear polarization of Y21M fd bacteriophage and purple membrane. J. Am. Chem. Soc. 123:1010-11
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1010-1011
    • Rosay, M.1    Zeri, A.C.2    Astrof, N.S.3    Opella, S.J.4    Herzfeld, J.5    Griffin, R.G.6
  • 94
    • 82555187191 scopus 로고    scopus 로고
    • Neurotoxin II bound to acetylcholine receptors in native membranes studied by dynamic nuclear polarizationNMR
    • Linden AH, Lange S, Franks WT, Akbey U, Specker E, et al. 2011. Neurotoxin II bound to acetylcholine receptors in native membranes studied by dynamic nuclear polarizationNMR. J. Am. Chem. Soc. 133:19266-69
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 19266-19269
    • Linden, A.H.1    Lange, S.2    Franks, W.T.3    Akbey, U.4    Specker, E.5
  • 95
  • 96
    • 0017231964 scopus 로고
    • Photoreceptor protein from the purplemembrane of Halobacterium halobium: Molecular weight and retinal binding site
    • Bridgen J,Walker ID. 1976. Photoreceptor protein from the purplemembrane of Halobacterium halobium: molecular weight and retinal binding site. Biochemistry 15:792-98
    • (1976) Biochemistry , vol.15 , pp. 792-798
    • Bridgen Jwalker, I.D.1
  • 98
    • 84858275751 scopus 로고    scopus 로고
    • Solid-stateNMRspectroscopy on cellular preparations enhanced by dynamic nuclear polarization
    • RenaultM, Pawsey S, Bos MP, Koers EJ,NandD, et al. 2012. Solid-stateNMRspectroscopy on cellular preparations enhanced by dynamic nuclear polarization. Angew. Chem. Int. Ed. Engl. 51:2998-3001
    • (2012) Angew. Chem. Int. Ed. Engl. , vol.51 , pp. 2998-3001
    • Renault, M.1    Pawsey, S.2    Bos, M.P.3    Koers, E.J.4    Nand, D.5
  • 101
    • 77950355556 scopus 로고    scopus 로고
    • In situ high-field dynamic nuclear polarization: Direct and indirect polarization of 13C nuclei
    • Maly T, Miller AF, Griffin RG. 2010. In situ high-field dynamic nuclear polarization: direct and indirect polarization of 13C nuclei. ChemPhysChem 11:999-1001
    • (2010) ChemPhysChem , vol.11 , pp. 999-1001
    • Maly, T.1    Miller, A.F.2    Griffin, R.G.3
  • 104
    • 55049102570 scopus 로고    scopus 로고
    • Biomolecular solid state NMR with magic-angle spinning at 25 K
    • Thurber KR, Tycko R. 2008. Biomolecular solid state NMR with magic-angle spinning at 25 K. J. Magn. Reson. 195:179-86
    • (2008) J. Magn. Reson. , vol.195 , pp. 179-186
    • Thurber, K.R.1    Tycko, R.2
  • 105
    • 84863115526 scopus 로고    scopus 로고
    • Rigid orthogonal bis-TEMPO biradicals with improved solubility for dynamic nuclear polarization
    • Dane EL, Corzilius B, Rizzato E, Stocker P, Maly T, et al. 2012. Rigid orthogonal bis-TEMPO biradicals with improved solubility for dynamic nuclear polarization. J. Org. Chem. 77:1789-97
    • (2012) J. Org. Chem. , vol.77 , pp. 1789-1797
    • Dane, E.L.1    Corzilius, B.2    Rizzato, E.3    Stocker, P.4    Maly, T.5
  • 107
    • 79954449786 scopus 로고    scopus 로고
    • Suppression of phospholipid biosynthesis by cerulenin in the condensed single-protein-production (cSPP) system
    • Mao LL, Inoue K, Tao YS, Montelione GT, McDermott AE, Inouye M. 2011. Suppression of phospholipid biosynthesis by cerulenin in the condensed single-protein-production (cSPP) system. J. Biomol. NMR 49:131-37
    • (2011) J. Biomol. NMR , vol.49 , pp. 131-137
    • Mao, L.L.1    Inoue, K.2    Tao, Y.S.3    Montelione, G.T.4    McDermott, A.E.5    Inouye, M.6
  • 108
    • 71049165894 scopus 로고    scopus 로고
    • Production of membrane proteins for NMR studies using the condensed single protein (cSPP) production system
    • Mao L, Tang Y, Vaiphei ST, Shimazu T, Kim SG, et al. 2009. Production of membrane proteins for NMR studies using the condensed single protein (cSPP) production system. J. Struct. Funct. Genomics 10:281-89
    • (2009) J. Struct. Funct. Genomics , vol.10 , pp. 281-289
    • Mao, L.1    Tang, Y.2    Vaiphei, S.T.3    Shimazu, T.4    Kim, S.G.5
  • 109
    • 77951297414 scopus 로고    scopus 로고
    • The E. coli single protein production system for production and structural analysis of membrane proteins
    • MaoL, Vaiphei ST, Shimazu T, SchneiderWM,TangY, et al. 2010. The E. coli single protein production system for production and structural analysis of membrane proteins. J. Struct. Funct. Genomics 11:81-84
    • (2010) J. Struct. Funct. Genomics , vol.11 , pp. 81-84
    • Maol Vaiphei, S.T.1    Shimazu, T.2    Schneider, W.M.3    Tang, Y.4
  • 111
    • 84862703873 scopus 로고    scopus 로고
    • 1H dynamic nuclear polarization based on an endogenous radical
    • Maly T, Cui D, Griffin RG, Mille A. 2012. 1H dynamic nuclear polarization based on an endogenous radical. J. Phys. Chem. B 116:7055-65
    • (2012) J. Phys. Chem. B , vol.116 , pp. 7055-7065
    • Maly, T.1    Cui, D.2    Griffin, R.G.3    Mille, A.4
  • 112
    • 85012754454 scopus 로고
    • Dynamic nuclear polarization in liquids
    • Hausser KH, Stehlik D. 1968. Dynamic nuclear polarization in liquids. Adv. Magn. Reson. 3:79-139
    • (1968) Adv. Magn. Reson. , vol.3 , pp. 79-139
    • Hausser, K.H.1    Stehlik, D.2
  • 113
    • 68349090260 scopus 로고    scopus 로고
    • Dynamic nuclear polarization of water by a nitroxide radical: Rigorous treatment of the electron spin saturation and comparison with experiments at 9.2 Tesla
    • Sezer D, Gafurov M, Prandolini MJ, Denysenkov VP, Prisner TF. 2009. Dynamic nuclear polarization of water by a nitroxide radical: rigorous treatment of the electron spin saturation and comparison with experiments at 9.2 Tesla. Phys. Chem. Chem. Phys. 11:6638-53
    • (2009) Phys. Chem. Chem. Phys. , vol.11 , pp. 6638-6653
    • Sezer, D.1    Gafurov, M.2    Prandolini, M.J.3    Denysenkov, V.P.4    Prisner, T.F.5
  • 114
    • 77952937685 scopus 로고    scopus 로고
    • Water 1H relaxation dispersion analysis on a nitroxide radical provides information on the maximal signal enhancement inOverhauser dynamic nuclear polarization experiments
    • Bennati M, Luchinat C, Parigi G, Turke MT. 2010. Water 1H relaxation dispersion analysis on a nitroxide radical provides information on the maximal signal enhancement inOverhauser dynamic nuclear polarization experiments. Phys. Chem. Chem. Phys. 12:5902-10
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 5902-5910
    • Bennati, M.1    Luchinat, C.2    Parigi, G.3    Turke, M.T.4
  • 115
    • 79952419942 scopus 로고    scopus 로고
    • Saturation factor of nitroxide radicals in liquid DNP by pulsed ELDOR experiments
    • Turke MT, Bennati M. 2011. Saturation factor of nitroxide radicals in liquid DNP by pulsed ELDOR experiments. Phys. Chem. Chem. Phys. 13:3630-33
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 3630-3633
    • Turke, M.T.1    Bennati, M.2
  • 116
    • 0000807746 scopus 로고
    • Dynamic effects of pair correlation functions on spin relaxation by translational diffusion in liquids
    • Hwang LP, Freed JH. 1975. Dynamic effects of pair correlation functions on spin relaxation by translational diffusion in liquids. J. Chem. Phys. 63:4017-25
    • (1975) J. Chem. Phys. , vol.63 , pp. 4017-4025
    • Hwang, L.P.1    Freed, J.H.2
  • 117
    • 0000265605 scopus 로고    scopus 로고
    • Interactions of hydration water and biological membranes studied by neutron scattering
    • Fitter J, Lechner RE, Dencher NA. 1999. Interactions of hydration water and biological membranes studied by neutron scattering. J. Phys. Chem. B 103:8036-50
    • (1999) J. Phys. Chem. B , vol.103 , pp. 8036-8050
    • Fitter, J.1    Lechner, R.E.2    Dencher, N.A.3
  • 118
    • 0030057862 scopus 로고    scopus 로고
    • The influence of a protein on water dynamics in its vicinity investigated by molecular dynamics simulation
    • Abseher R, Schreiber H, Steinhauser O. 1996. The influence of a protein on water dynamics in its vicinity investigated by molecular dynamics simulation. Proteins Struct. Funct. Genet. 25:366-78
    • (1996) Proteins Struct. Funct. Genet. , vol.25 , pp. 366-378
    • Abseher, R.1    Schreiber, H.2    Steinhauser, O.3
  • 119
    • 0027374170 scopus 로고
    • Rotational and translational water diffusion in the hemoglobin hydration shell: Dielectric and proton nuclear-relaxation measurements
    • Steinhoff HJ, Kramm B, Hess G, Owerdieck C, Redhardt A. 1993. Rotational and translational water diffusion in the hemoglobin hydration shell: dielectric and proton nuclear-relaxation measurements. Biophys. J. 65:1486-95
    • (1993) Biophys. J. , vol.65 , pp. 1486-1495
    • Steinhoff, H.J.1    Kramm, B.2    Hess, G.3    Owerdieck, C.4    Redhardt, A.5
  • 120
    • 36549099951 scopus 로고
    • Nitroxide radical induced solvent proton relaxation: Measurement of localized translational diffusion
    • Polnaszek CF, Bryant RG. 1984. Nitroxide radical induced solvent proton relaxation: measurement of localized translational diffusion. J. Chem. Phys. 81:4038-45
    • (1984) J. Chem. Phys. , vol.81 , pp. 4038-4045
    • Polnaszek, C.F.1    Bryant, R.G.2
  • 121
    • 68349111782 scopus 로고    scopus 로고
    • Site-specific dynamic nuclear polarization of hydration water as a generally applicable approach to monitor protein aggregation
    • Pavlova A, McCarney ER, Peterson DW, Dahlquist FW, Lew J, Han S. 2009. Site-specific dynamic nuclear polarization of hydration water as a generally applicable approach to monitor protein aggregation. Phys. Chem. Chem. Phys. 11:6833-39
    • (2009) Phys. Chem. Chem. Phys. , vol.11 , pp. 6833-6839
    • Pavlova, A.1    McCarney, E.R.2    Peterson, D.W.3    Dahlquist, F.W.4    Lew, J.5    Han, S.6
  • 122
    • 84857058205 scopus 로고    scopus 로고
    • An ultrasensitive tool exploiting hydration dynamics to decipher weak lipid membrane-polymer interactions
    • Cheng CY, Wang JY, Kausik R, Lee KY, Han S. 2012. An ultrasensitive tool exploiting hydration dynamics to decipher weak lipid membrane-polymer interactions. J. Magn. Reson. 215:115- 19
    • (2012) J. Magn. Reson. , vol.215 , pp. 115-119
    • Cheng, C.Y.1    Wang, J.Y.2    Kausik, R.3    Lee, K.Y.4    Han, S.5
  • 123
    • 73249129520 scopus 로고    scopus 로고
    • Ultrasensitive detection of interfacial diffusion coefficient on lipid vesicle surfaces at molecular length scales
    • Kausik R,Han S. 2009. Ultrasensitive detection of interfacial diffusion coefficient on lipid vesicle surfaces at molecular length scales. J. Am. Chem. Soc. 131:18254-56
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 18254-18256
    • Kausik Rhan, S.1
  • 124
    • 79956007018 scopus 로고    scopus 로고
    • Dynamics and state of lipid bilayer-internal water unraveled with solution state 1H dynamic nuclear polarization
    • Kausik R, Han S. 2011. Dynamics and state of lipid bilayer-internal water unraveled with solution state 1H dynamic nuclear polarization. Phys. Chem. Chem. Phys. 13:7732-46
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 7732-7746
    • Kausik, R.1    Han, S.2
  • 125
    • 70350025178 scopus 로고    scopus 로고
    • Local water dynamics in coacervated polyelectrolytes monitored through dynamic nuclear polarization-enhanced 1H NMR
    • Kausik R, Srivastava A, Korevaar PA, Stucky G,Waite JH, Han S. 2009. Local water dynamics in coacervated polyelectrolytes monitored through dynamic nuclear polarization-enhanced 1H NMR. Macromolecules 42:7404-12
    • (2009) Macromolecules , vol.42 , pp. 7404-7412
    • Kausik, R.1    Srivastava, A.2    Korevaar, P.A.3    Stucky Gwaite, J.H.4    Han, S.5
  • 126
    • 84866100040 scopus 로고    scopus 로고
    • Nature of interactions between PEO-PPO-PEO triblock copolymers and lipid membranes: (II) Role of hydration dynamics revealed by dynamic nuclear polarization
    • Cheng CY, Wang J, Kausik R, Lee KYC,Han S. 2012. Nature of interactions between PEO-PPO-PEO triblock copolymers and lipid membranes: (II) role of hydration dynamics revealed by dynamic nuclear polarization. Biomacromolecules 13:2624-33
    • (2012) Biomacromolecules , vol.13 , pp. 2624-2633
    • Cheng, C.Y.1    Wang, J.2    Kausik, R.3    Lee, K.Y.C.4    Han, S.5
  • 127
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim PS, Baldwin RL. 1990. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59:631-60
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 128
    • 79953765150 scopus 로고    scopus 로고
    • Solid-state NMR studies of amyloid fibril structure
    • Tycko R. 2011. Solid-state NMR studies of amyloid fibril structure. Annu. Rev. Phys. Chem. 62:279-99
    • (2011) Annu. Rev. Phys. Chem. , vol.62 , pp. 279-299
    • Tycko, R.1
  • 130
    • 77950283310 scopus 로고    scopus 로고
    • Studying the stoichiometries of membrane proteins by mass spectrometry: Microbial rhodopsins and a potassium ion channel
    • Hoffmann J, Aslimovska L, Bamann C, Glaubitz C, Bamberg E, Brutschy B. 2010. Studying the stoichiometries of membrane proteins by mass spectrometry: microbial rhodopsins and a potassium ion channel. Phys. Chem. Chem. Phys. 12:3480-85
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 3480-3485
    • Hoffmann, J.1    Aslimovska, L.2    Bamann, C.3    Glaubitz, C.4    Bamberg, E.5    Brutschy, B.6
  • 131
    • 84865117903 scopus 로고    scopus 로고
    • Liquid stateDNPfor water accessibility measurements on spin-labeled membrane proteins at physiological temperatures
    • Doll A, Bordignon E, Joseph B,Tschaggelar R, JeschkeG. 2012. Liquid stateDNPfor water accessibility measurements on spin-labeled membrane proteins at physiological temperatures. J. Magn. Reson. 222:34- 43
    • (2012) J. Magn. Reson. , vol.222 , pp. 34-43
    • Doll, A.1    Bordignon, E.2    Tschaggelar, B.3    Jeschke, G.4
  • 132
    • 0017896443 scopus 로고
    • Laser photo-CIDNP as a surface probe for proteins in solution
    • Kaptein R, Dijkstra K,Nicolay K. 1978. Laser photo-CIDNP as a surface probe for proteins in solution. Nature 274:293-94
    • (1978) Nature , vol.274 , pp. 293-294
    • Kaptein, R.1    Dijkstra, K.2    Nicolay, K.3
  • 133
    • 80055013409 scopus 로고    scopus 로고
    • A 10,000-fold nuclear hyperpolarization of a membrane protein in the liquid phase via a solid-state mechanism
    • Daviso E, Janssen GJ, Alia A, Jeschke G, Matysik J, Tessari M. 2011. A 10,000-fold nuclear hyperpolarization of a membrane protein in the liquid phase via a solid-state mechanism. J. Am. Chem. Soc. 133:16754-57
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 16754-16757
    • Daviso, E.1    Janssen, G.J.2    Alia, A.3    Jeschke, G.4    Matysik, J.5    Tessari, M.6
  • 134
    • 79957682366 scopus 로고    scopus 로고
    • 1H-detected 13C photo-CIDNP as a sensitivity enhancement tool in solution NMR
    • Lee JH, Sekhar A, Cavagnero S. 2011. 1H-detected 13C photo-CIDNP as a sensitivity enhancement tool in solution NMR. J. Am. Chem. Soc. 133:8062-65
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 8062-8065
    • Lee, J.H.1    Sekhar, A.2    Cavagnero, S.3
  • 135
    • 67149123665 scopus 로고    scopus 로고
    • 1H photo-CIDNP enhancements in heteronuclear correlation NMR spectroscopy
    • Sekhar A, Cavagnero S. 2009. 1H photo-CIDNP enhancements in heteronuclear correlation NMR spectroscopy. J. Phys. Chem. B 113:8310-18
    • (2009) J. Phys. Chem. B , vol.113 , pp. 8310-8318
    • Sekhar, A.1    Cavagnero, S.2
  • 136
    • 77952892386 scopus 로고    scopus 로고
    • Optimization of dynamic nuclear polarization experiments in aqueous solution at 15 MHz/9.7 GHz: A comparative study with DNP at 140 MHz/94 GHz
    • TurkeMT, Tkach I, ReeseM,Hofer P, Bennati M. 2010. Optimization of dynamic nuclear polarization experiments in aqueous solution at 15 MHz/9.7 GHz: A comparative study with DNP at 140 MHz/94 GHz. Phys. Chem. Chem. Phys. 12:5893-901
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 5893-5901
    • Turkemt Tkach, I.1    Reesemhofer, P.2    Bennati, M.3
  • 137
    • 84868565934 scopus 로고    scopus 로고
    • Quantitative analysis of molecular transport across liposomal bilayer by J-mediated 13C Overhauser dynamic nuclear polarization
    • Cheng CY, Goor OJGM, Han S. 2012. Quantitative analysis of molecular transport across liposomal bilayer by J-mediated 13C Overhauser dynamic nuclear polarization. Anal. Chem. 84:8936-40
    • (2012) Anal. Chem. , vol.84 , pp. 8936-8940
    • Cheng, C.Y.1    Ojgm, G.2    Han, S.3
  • 138
    • 84865294387 scopus 로고    scopus 로고
    • Mapping membrane protein structure with fluorescence
    • Taraska JW. 2012. Mapping membrane protein structure with fluorescence. Curr. Opin. Struct. Biol. 22:507-13
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 507-513
    • Taraska, J.W.1
  • 139
    • 33645798851 scopus 로고    scopus 로고
    • The fluorescent toolbox for assessing protein location and function
    • Giepmans BNG, Adams SR, Ellisman MH, Tsien RY. 2006. The fluorescent toolbox for assessing protein location and function. Science 312:217-24
    • (2006) Science , vol.312 , pp. 217-224
    • Bng, G.1    Adams, S.R.2    Ellisman, M.H.3    Tsien, R.Y.4
  • 140
    • 77952402284 scopus 로고    scopus 로고
    • Single-molecule dynamics of gating in a neurotransmitter transporter homologue
    • Zhao YF, Terry D, Shi L, Weinstein H, Blanchard SC, Javitch JA. 2010. Single-molecule dynamics of gating in a neurotransmitter transporter homologue. Nature 465:188-93
    • (2010) Nature , vol.465 , pp. 188-193
    • Zhao, Y.F.1    Terry, D.2    Shi, L.3    Weinstein, H.4    Blanchard, S.C.5    Javitch, J.A.6
  • 141
    • 84855455990 scopus 로고    scopus 로고
    • Antiparallel EmrE exports drugs by exchanging between asymmetric structures
    • Morrison EA, DeKoster GT, Dutta S, Vafabakhsh R, Clarkson MW, et al. 2012. Antiparallel EmrE exports drugs by exchanging between asymmetric structures. Nature 481:45-50
    • (2012) Nature , vol.481 , pp. 45-50
    • Morrison, E.A.1    Dekoster, G.T.2    Dutta, S.3    Vafabakhsh, R.4    Clarkson, M.W.5
  • 145
    • 79957962090 scopus 로고    scopus 로고
    • Residue-specific vibrational echoes yield 3D structures of a transmembrane helix dimmer
    • Remorino A, Korendovych IV, Wu Y, DeGrado WF, Hochstrasser RM. 2011. Residue-specific vibrational echoes yield 3D structures of a transmembrane helix dimer. Science 332:1206-9
    • (2011) Science , vol.332 , pp. 1206-1209
    • Remorino, A.1    Korendovych, I.V.2    Wu, Y.3    Degrado, W.F.4    Hochstrasser, R.M.5
  • 146
    • 84988117910 scopus 로고
    • Molecular motions and interactions as studied by dynamic nuclear polarization (DNP) in free-radical solutions
    • Mullerwarmuth W, Meisegresch K. 1983. Molecular motions and interactions as studied by dynamic nuclear polarization (DNP) in free-radical solutions. Adv. Magn. Reson. 11:1-45
    • (1983) Adv. Magn. Reson. , vol.11 , pp. 1-45
    • Mullerwarmuth, W.1    Meisegresch, K.2
  • 148
    • 0037205873 scopus 로고    scopus 로고
    • Solution-state dynamic nuclear polarization at high magnetic field
    • Loening NM, Rosay M, Weis V, Griffin RG. 2002. Solution-state dynamic nuclear polarization at high magnetic field. J. Am. Chem. Soc. 124:8808-9
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 8808-8809
    • Loening, N.M.1    Rosay, M.2    Weis, V.3    Griffin, R.G.4
  • 149
    • 68349119054 scopus 로고    scopus 로고
    • Dynamic nuclear polarization coupling factors calculated from molecular dynamics simulations of a nitroxide radical in water
    • Sezer D, Prandolini MJ, Prisner TF. 2009. Dynamic nuclear polarization coupling factors calculated from molecular dynamics simulations of a nitroxide radical in water. Phys. Chem. Chem. Phys. 11:6626-37
    • (2009) Phys. Chem. Chem. Phys. , vol.11 , pp. 6626-6637
    • Sezer, D.1    Prandolini, M.J.2    Prisner, T.F.3
  • 150
    • 41449094103 scopus 로고    scopus 로고
    • Field dependent dynamic nuclear polarization with radicals in aqueous solution
    • Hofer P, Parigi G, Luchinat C, Carl P, Guthausen G, et al. 2008. Field dependent dynamic nuclear polarization with radicals in aqueous solution. J. Am. Chem. Soc. 130:3254-55
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 3254-3255
    • Hofer, P.1    Parigi, G.2    Luchinat, C.3    Carl, P.4    Guthausen, G.5
  • 152
    • 84873535860 scopus 로고    scopus 로고
    • Transmembrane protein activation refined by site-specific hydration dynamics
    • In press
    • Hussein S, Franck JM,Han S. 2013. Transmembrane protein activation refined by site-specific hydration dynamics. Angew. Chem. Int. Ed. Engl. In press
    • (2013) Angew. Chem. Int. Ed. Engl.
    • Hussein, S.1    Franck Jmhan, S.2


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