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Volumn 35, Issue 4, 1996, Pages 497-505

1H magnetic cross-relaxation between multiple solvent components and rotationally immobilized protein

Author keywords

cross relaxation; magnetization transfer; preferential solvation; protein solvation; Z spectroscopy

Indexed keywords

ACETONE; BINDING SITES; EFFICIENCY; MAGNETIZATION; MAMMALS; MOLECULES; ORGANIC SOLVENTS; SOLVATION; TEMPERATURE DISTRIBUTION;

EID: 0029658915     PISSN: 07403194     EISSN: None     Source Type: Journal    
DOI: 10.1002/mrm.1910350408     Document Type: Article
Times cited : (21)

References (45)
  • 2
    • 0018084374 scopus 로고
    • Magnetic cross-relaxation among protons in protein solution
    • S. H. Koenig, R. G. Bryant, K. Hallenga, G. S. Jacobs, Magnetic cross-relaxation among protons in protein solution. Biochemistry 17, 4348-4358 (1978).
    • (1978) Biochemistry , vol.17 , pp. 4348-4358
    • Koenig, S.H.1    Bryant, R.G.2    Hallenga, K.3    Jacobs, G.S.4
  • 3
    • 0017576498 scopus 로고
    • Cross relaxation and spin diffusion in the proton nmr of hydrated collagen
    • H. T. Edzes, E. T. Samulski, Cross relaxation and spin diffusion in the proton nmr of hydrated collagen. Nature 265, 521-523 (1977).
    • (1977) Nature , vol.265 , pp. 521-523
    • Edzes, H.T.1    Samulski, E.T.2
  • 4
    • 49349118272 scopus 로고
    • The measurement of cross-relaxation effects in the proton nmr spin-lattice relaxation of water in biological systems: Hydrated collagen and muscle
    • H. T. Edzes, E. T. Samulski, The measurement of cross-relaxation effects in the proton nmr spin-lattice relaxation of water in biological systems: hydrated collagen and muscle. J. Magn. Reson. 31, 207-229 (1978).
    • (1978) J. Magn. Reson. , vol.31 , pp. 207-229
    • Edzes, H.T.1    Samulski, E.T.2
  • 5
    • 0017692405 scopus 로고
    • NMR relaxation in cross-linked lysozyme crystals: An isotope dilution experiment
    • E. Hsi, R. G. Bryant, NMR relaxation in cross-linked lysozyme crystals: an isotope dilution experiment. Arch. Biochem. Biophys. 183, 588-591 (1977).
    • (1977) Arch. Biochem. Biophys. , vol.183 , pp. 588-591
    • Hsi, E.1    Bryant, R.G.2
  • 6
    • 0001727861 scopus 로고
    • Proton-nuclear spin relaxation and molecular dynamics in the lysozyme-water system
    • W. E. Shirley, R. G. Bryant, Proton-nuclear spin relaxation and molecular dynamics in the lysozyme-water system. J. Am. Chem. Soc. 104, 2910-2918 (1982).
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 2910-2918
    • Shirley, W.E.1    Bryant, R.G.2
  • 7
    • 0007707294 scopus 로고
    • Cross relaxation in hydrated collagen
    • B. M. Fung, T. W. McGauhy, Cross relaxation in hydrated collagen. J. Magn. Reson. 39, 413-420 (1980).
    • (1980) J. Magn. Reson. , vol.39 , pp. 413-420
    • Fung, B.M.1    McGauhy, T.W.2
  • 8
    • 0024573913 scopus 로고
    • Magnetization transfer contrast (mtc) and tissue water proton relaxation in vivo
    • S. D. Wolff, R. S. Balaban, Magnetization transfer contrast (mtc) and tissue water proton relaxation in vivo. Magn. Reson. Med. 10, 135-144 (1989).
    • (1989) Magn. Reson. Med. , vol.10 , pp. 135-144
    • Wolff, S.D.1    Balaban, R.S.2
  • 9
    • 0026021984 scopus 로고
    • Applications of nuclear magnetic cross-relaxation spectroscopy to tissues
    • J. Grad, D. Mendelson, F. Hyder, R. G. Bryant, Applications of nuclear magnetic cross-relaxation spectroscopy to tissues. Magn. Reson. Med. 17, 452-459 (1991).
    • (1991) Magn. Reson. Med. , vol.17 , pp. 452-459
    • Grad, J.1    Mendelson, D.2    Hyder, F.3    Bryant, R.G.4
  • 10
    • 0002047889 scopus 로고
    • Nuclear magnetic cross relaxation spectroscopy
    • J.Grad, R. G. Bryant. Nuclear magnetic cross relaxation spectroscopy. J. Magn. Reson. 90, 1-8 (1990).
    • (1990) J. Magn. Reson. , vol.90 , pp. 1-8
    • Grad, J.1    Bryant, R.G.2
  • 11
    • 0025836605 scopus 로고
    • Water-proton nuclear magnetic relaxation in heterogeneous systems: Hydrated lysozyme results
    • C. C. Lester, R. G. Bryant, Water-proton nuclear magnetic relaxation in heterogeneous systems: hydrated lysozyme results. Magn. Reson. Med. 22, 143-153 (1991).
    • (1991) Magn. Reson. Med. , vol.22 , pp. 143-153
    • Lester, C.C.1    Bryant, R.G.2
  • 12
    • 0026002876 scopus 로고
    • The magnetic field dependence of proton spin relaxation in tissues
    • R. G. Bryant, D. A. Mendelson, C. C. Lester, The magnetic field dependence of proton spin relaxation in tissues. Magn. Reson. Med. 21, 117-126 (1991).
    • (1991) Magn. Reson. Med. , vol.21 , pp. 117-126
    • Bryant, R.G.1    Mendelson, D.A.2    Lester, C.C.3
  • 13
    • 0025925024 scopus 로고
    • Quantitative 1H magnetization transfer in vivo
    • J. Eng, T. L. Ceckler, R. S. Balaban. Quantitative 1H magnetization transfer in vivo. Magn. Reson. Med. 17, 304-314 (1991).
    • (1991) Magn. Reson. Med. , vol.17 , pp. 304-314
    • Eng, J.1    Ceckler, T.L.2    Balaban, R.S.3
  • 15
    • 85092120478 scopus 로고    scopus 로고
    • 1 in the rotating frame
    • (I. R. Young, Ed.), Wiley, New York, in press
    • 1 in the rotating frame, "Encyclopedia of Magnetic Resonance" (I. R. Young, Ed.), Wiley, New York, in press.
    • Encyclopedia of Magnetic Resonance
    • Balaban, R.1
  • 16
    • 0002369196 scopus 로고    scopus 로고
    • Magnetization transfer and cross-relaxation in tissue
    • (I. R. Young, Ed.), Wiley, New York, in press
    • R. G. Bryant, Magnetization transfer and cross-relaxation in tissue, in "Encyclopedia of NMR" (I. R. Young, Ed.), Wiley, New York, in press.
    • Encyclopedia of NMR
    • Bryant, R.G.1
  • 17
    • 0003317458 scopus 로고    scopus 로고
    • Magnetization transfer contrast: Clinical applications
    • (I. R. Young, Ed.), Wiley, New York, in press
    • R. Baudouin, Magnetization transfer contrast: clinical applications, in "Encyclopedia of NMR" (I. R. Young, Ed.), Wiley, New York, in press.
    • Encyclopedia of NMR
    • Baudouin, R.1
  • 18
    • 0041442515 scopus 로고
    • Nuclear magnetic relaxation dispersion in protein solutions: A test of proton-exchange coupling
    • R. G. Bryant, M. Jarvis, Nuclear magnetic relaxation dispersion in protein solutions: a test of proton-exchange coupling. J. Phys. Chem. 88, 1323-1324 (1984).
    • (1984) J. Phys. Chem. , vol.88 , pp. 1323-1324
    • Bryant, R.G.1    Jarvis, M.2
  • 19
    • 0028014341 scopus 로고
    • Magnetization transfer affects the proton creatine/phosphocreatine signal intensity: In vivo demonstration in the rat brain
    • W. Dreher, D. G. Norris, D. Leibfritz, Magnetization transfer affects the proton creatine/phosphocreatine signal intensity: in vivo demonstration in the rat brain. Magn. Reson. Med. 31, 81-84 (1994).
    • (1994) Magn. Reson. Med. , vol.31 , pp. 81-84
    • Dreher, W.1    Norris, D.G.2    Leibfritz, D.3
  • 20
    • 0001534866 scopus 로고
    • Lineshape of magnetization transfer via cross relaxation
    • X. Wu, Lineshape of magnetization transfer via cross relaxation. J. Magn. Reson. 94, 186-190 (1991).
    • (1991) J. Magn. Reson. , vol.94 , pp. 186-190
    • Wu, X.1
  • 21
    • 44949270768 scopus 로고
    • Incorporation of magnetization transfer into the formalism for rotating-frame spin-lattice proton nmr relaxation in the presence of an off-resonance irradiation field
    • G. H. Caines, T.Schleich, J. M. Rydzewski, Incorporation of magnetization transfer into the formalism for rotating-frame spin-lattice proton nmr relaxation in the presence of an off-resonance irradiation field. J. Magn. Reson. 95, 558-566 (1991).
    • (1991) J. Magn. Reson. , vol.95 , pp. 558-566
    • Caines, G.H.1    Schleich, T.2    Rydzewski, J.M.3
  • 22
    • 0000628419 scopus 로고
    • Transfer decay of longitudianl magnetization in heterogeneous spin systems under selective saturation
    • H. N. Yeung, S. D. Swanson, Transfer decay of longitudianl magnetization in heterogeneous spin systems under selective saturation. J. Magn. Reson. 99, 466-479 (1992).
    • (1992) J. Magn. Reson. , vol.99 , pp. 466-479
    • Yeung, H.N.1    Swanson, S.D.2
  • 24
    • 0002541149 scopus 로고
    • Transient decay of longitudinal magnetization in heterogeneous spin systems under selective saturation. IV. Reformulation of the spinbath-model equations by the Redfield-Provotorov theory
    • H. N. Yeung, R. S. Adler, S. D. Swanson. Transient decay of longitudinal magnetization in heterogeneous spin systems under selective saturation. IV. Reformulation of the spinbath-model equations by the Redfield-Provotorov theory. J. Magn. Reson. Series A. 106, 37-45 (1994).
    • (1994) J. Magn. Reson. Series A , vol.106 , pp. 37-45
    • Yeung, H.N.1    Adler, R.S.2    Swanson, S.D.3
  • 25
    • 0027965945 scopus 로고
    • Transition from Lorentzian to Gaussian line shape of magnetization transfer spectrum in bovine serum albumin solutions
    • M. Iino. Transition from Lorentzian to Gaussian line shape of magnetization transfer spectrum in bovine serum albumin solutions. Magn. Reson. Med. 32, 459-463 (1994).
    • (1994) Magn. Reson. Med. , vol.32 , pp. 459-463
    • Iino, M.1
  • 26
    • 0005155106 scopus 로고
    • Transient decay of longitudinal magnetization in heterogeneous spin systems under selective saturation. III. Solution by projection operators
    • R. S. Adler H. N. Yeung, Transient decay of longitudinal magnetization in heterogeneous spin systems under selective saturation. III. Solution by projection operators. J. Magn. Reson. Series A. 104, 321-330 (1993).
    • (1993) J. Magn. Reson. Series A , vol.104 , pp. 321-330
    • Adler, R.S.1    Yeung, H.N.2
  • 27
    • 0005108174 scopus 로고
    • Transient responses of a heterogeneous spin system to binomial pulse saturation
    • H. N. Yeung, Transient responses of a heterogeneous spin system to binomial pulse saturation. J. Magn. Reson. Series A. 102, 8-5 (1993).
    • (1993) J. Magn. Reson. Series A , vol.102 , pp. 8-15
    • Yeung, H.N.1
  • 28
    • 0028437434 scopus 로고
    • Relaxation-matrix formalism for rotating-frame spin-lattice NMR relaxation and magnetization transfer in the presence of an off-resonance irradiation field
    • K. Kuwata, D. Brooks, H. Yang, T. Schleich. Relaxation-matrix formalism for rotating-frame spin-lattice NMR relaxation and magnetization transfer in the presence of an off-resonance irradiation field. J. Magn. Reson. Series B. 104, 11-25 (1994).
    • (1994) J. Magn. Reson. Series B , vol.104 , pp. 11-25
    • Kuwata, K.1    Brooks, D.2    Yang, H.3    Schleich, T.4
  • 31
    • 0028144010 scopus 로고
    • Magnetization transfer, cross-relaxation, and chemical exchange in rotationally immobilized protein gels
    • D. Zhou, R. G. Bryant, Magnetization transfer, cross-relaxation, and chemical exchange in rotationally immobilized protein gels. Magn. Reson. Med. 32, 725-732 (1994).
    • (1994) Magn. Reson. Med. , vol.32 , pp. 725-732
    • Zhou, D.1    Bryant, R.G.2
  • 32
    • 0000464950 scopus 로고
    • Self diffusion of water at the protein surface: A measurement
    • C. F. Polnaszek, R. G. Bryant, Self diffusion of water at the protein surface: a measurement. J. Am. Chem. Soc. 106, 428-429 (1984).
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 428-429
    • Polnaszek, C.F.1    Bryant, R.G.2
  • 33
    • 36549099951 scopus 로고
    • Nitroxide radical induced solvent proton relaxation: Measurement of localized translational diffusion
    • C. F. Polnaszek, R. G. Bryant, Nitroxide radical induced solvent proton relaxation: measurement of localized translational diffusion. J. Chem. Phys. 81, 4038-4045 (1984).
    • (1984) J. Chem. Phys. , vol.81 , pp. 4038-4045
    • Polnaszek, C.F.1    Bryant, R.G.2
  • 34
    • 0001699290 scopus 로고
    • NMR study of diffusiion in protein hydration shells
    • R. Kimmich, NMR study of diffusiion in protein hydration shells. Prog. Colloid. Polym. 83, 211-215 (1990).
    • (1990) Prog. Colloid. Polym. , vol.83 , pp. 211-215
    • Kimmich, R.1
  • 35
    • 0009930531 scopus 로고
    • Nuclear magnetic relaxation dispersion measurement of water mobility at a silica surface
    • C. F. Polnaszek, D. Hanggi, P. W. Carr, R. G. Bryant, Nuclear magnetic relaxation dispersion measurement of water mobility at a silica surface. Anal Chem. Acta 194, 311-316 (1987).
    • (1987) Anal Chem. Acta , vol.194 , pp. 311-316
    • Polnaszek, C.F.1    Hanggi, D.2    Carr, P.W.3    Bryant, R.G.4
  • 36
    • 0000857486 scopus 로고
    • Studies of protein hydration in aqueous solution by direct NMR observation of individual protein-bound water molecules
    • G. Ottig, K.Wuthrich, Studies of protein hydration in aqueous solution by direct NMR observation of individual protein-bound water molecules. J. Am. Chem. Soc. 111, 1871-1888 (1989).
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 1871-1888
    • Ottig, G.1    Wuthrich, K.2
  • 37
    • 0026193384 scopus 로고
    • Protein hydration studied with Homonuclear 3D 1H NMR experiments
    • G. Ottig, E. Liepinsh, B. T. I. I. Farmer, K. Wuthrich. Protein hydration studied with Homonuclear 3D 1H NMR experiments. J. Biol. NMR 1, 209-215 (1991).
    • (1991) J. Biol. NMR , vol.1 , pp. 209-215
    • Ottig, G.1    Liepinsh, E.2    Farmer, B.T.I.I.3    Wuthrich, K.4
  • 38
    • 0026326956 scopus 로고
    • Protein hydration in aqueous solution
    • G. Ottig, E. Liepinsh, K. Wuthrich, Protein hydration in aqueous solution. Science 254, 974-980 (1991).
    • (1991) Science , vol.254 , pp. 974-980
    • Ottig, G.1    Liepinsh, E.2    Wuthrich, K.3
  • 39
    • 84957316785 scopus 로고
    • Proton exchange with internal water molecules in the protein BPTI in aqueous solution
    • G. Otting, E. Liepinsh, K. Wuthrich, Proton exchange with internal water molecules in the protein BPTI in aqueous solution. J. Am. Chem. Soc. 113, 4363-4369 (1991).
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 4363-4369
    • Otting, G.1    Liepinsh, E.2    Wuthrich, K.3
  • 40
    • 12044251259 scopus 로고
    • Solvent suppression with symmetrically-shifted pulses
    • S. Smallcombe, Solvent suppression with symmetrically-shifted pulses. J. Am. Chem. Soc. 115, 4776-4785 (1993).
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 4776-4785
    • Smallcombe, S.1
  • 41
    • 0001770123 scopus 로고
    • Protein solvent interactions
    • S. N. Timasheff, Protein solvent interactions. Acc. Chem. Res. 3, 62-68 (1970).
    • (1970) Acc. Chem. Res. , vol.3 , pp. 62-68
    • Timasheff, S.N.1
  • 42
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • K. Dill, Dominant forces in protein folding. Biochemistry 29, 7134-7155 (1990).
    • (1990) Biochemistry , vol.29 , pp. 7134-7155
    • Dill, K.1
  • 44
    • 0018368695 scopus 로고
    • Hydrogen exchange kinetics and internal motions in proteins and nucleic acids
    • C. K. Woodward, B. D. Hilton, Hydrogen exchange kinetics and internal motions in proteins and nucleic acids. Ann. Rev. Biophys. Bioeng. 8, 99-128 (1979).
    • (1979) Ann. Rev. Biophys. Bioeng. , vol.8 , pp. 99-128
    • Woodward, C.K.1    Hilton, B.D.2
  • 45
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics in protein and nucleic acids
    • S. W. Englander, N. R. Kallenbach, Hydrogen exchange and structural dynamics in protein and nucleic acids. Q. Rev. Biophys. 16, 521-655 (1984)
    • (1984) Q. Rev. Biophys. , vol.16 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.