메뉴 건너뛰기




Volumn 84, Issue 1, 2003, Pages 558-563

Protein reorientation and bound water molecules measured by 1H magnetic spin-lattice relaxation

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; WATER;

EID: 0037215796     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74875-9     Document Type: Article
Times cited : (50)

References (21)
  • 2
    • 0029889510 scopus 로고    scopus 로고
    • The dynamics of water-protein interactions
    • Bryant, R. G. 1996a. The dynamics of water-protein interactions. Annu. Rev. Biophys. Biomol. Struct. 25:29-53.
    • (1996) Annu. Rev. Biophys. Biomol. Struct. , vol.25 , pp. 29-53
    • Bryant, R.G.1
  • 3
    • 0002369196 scopus 로고    scopus 로고
    • Magnetization transfer and cross relaxation in tissue
    • E. D. M. Grant and R. K. Harris, Editors. John Wiley, New York
    • Bryant, R. G. 1996b. Magnetization transfer and cross relaxation in tissue. In Encyclopedia of Magnetic Resonance. E. D. M. Grant and R. K. Harris, Editors. John Wiley, New York. 2954-2962.
    • (1996) Encyclopedia of Magnetic Resonance , pp. 2954-2962
    • Bryant, R.G.1
  • 4
    • 0028948786 scopus 로고
    • Protein hydration dynamics in aqueous solution: A comparison of bovine pancreatic trypsin inhibitor and ubiquitin by oxygen-17 spin relaxation dispersion
    • Denisov, V. P., and B. Halle. 1995. Protein hydration dynamics in aqueous solution: A comparison of bovine pancreatic trypsin inhibitor and ubiquitin by oxygen-17 spin relaxation dispersion. J. Mol. Biol. 245:682-697.
    • (1995) J. Mol. Biol. , vol.245 , pp. 682-697
    • Denisov, V.P.1    Halle, B.2
  • 5
    • 0030325741 scopus 로고    scopus 로고
    • Protein hydration dynamics in aqueous solution
    • Denisov, V. P., and B. Halle. 1996. Protein hydration dynamics in aqueous solution. Faraday Discuss. 103:227-244.
    • (1996) Faraday Discuss. , vol.103 , pp. 227-244
    • Denisov, V.P.1    Halle, B.2
  • 6
    • 0032580978 scopus 로고    scopus 로고
    • Thermal denaturation of ribonuclease A characterized by water oxygen-17 and deuterium magnetic relaxation dispersion
    • Denisov, V. P., and B. Halle. 1998. Thermal denaturation of ribonuclease A characterized by water oxygen-17 and deuterium magnetic relaxation dispersion. Biochemistry. 37:9595-9604.
    • (1998) Biochemistry , vol.37 , pp. 9595-9604
    • Denisov, V.P.1    Halle, B.2
  • 7
    • 0029081424 scopus 로고
    • Residence times of buried water molecules in bovine pancreatic trypsin inhibitor and its G36S mutant
    • Denisov, V. P., B. Halle, J. Peters, and H. D. Horlein. 1995. Residence times of buried water molecules in bovine pancreatic trypsin inhibitor and its G36S mutant. Biochemistry. 34:9046-9051.
    • (1995) Biochemistry , vol.34 , pp. 9046-9051
    • Denisov, V.P.1    Halle, B.2    Peters, J.3    Horlein, H.D.4
  • 8
    • 0019526265 scopus 로고
    • Hydrodynamic properties of complex, rigid, biological macromolecules: Theory and applications
    • Garcia de la Torre, J. G., and V. A. Bloomfield. 1981. Hydrodynamic properties of complex, rigid, biological macromolecules: Theory and applications. Q. Rev. Biophys. 14:81-139.
    • (1981) Q. Rev. Biophys. , vol.14 , pp. 81-139
    • Garcia de la Torre, J.G.1    Bloomfield, V.A.2
  • 9
    • 0000503877 scopus 로고
    • Protein hydration from water oxygen-17 magnetic relaxation
    • Halle, B., T. Anderson, S. Forsen, and B. Lindman. 1981. Protein hydration from water oxygen-17 magnetic relaxation. J. Am. Chem. Soc. 103:500-508.
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 500-508
    • Halle, B.1    Anderson, T.2    Forsen, S.3    Lindman, B.4
  • 10
    • 0000202632 scopus 로고    scopus 로고
    • Multinuclear relaxation dispersion studies of protein hydration
    • L. J. Berliner and N. R. Krishna, editors. Klewer Academic/Plenum Press, New York
    • Halle, B., V. P. Denisov, and K. Venu. 1999. Multinuclear relaxation dispersion studies of protein hydration. In Biological Magnetic Resonance, Vol. 17. L. J. Berliner and N. R. Krishna, editors. Klewer Academic/Plenum Press, New York. 419-484.
    • (1999) Biological Magnetic Resonance , vol.17 , pp. 419-484
    • Halle, B.1    Denisov, V.P.2    Venu, K.3
  • 11
    • 0034071764 scopus 로고    scopus 로고
    • Protein-bound water molecule counting by resolution of (1)H spin-lattice relaxation mechanisms
    • Kiihne, S., and R. G. Bryant. 2000. Protein-bound water molecule counting by resolution of (1)H spin-lattice relaxation mechanisms. Biophys. J. 78:2163-2169.
    • (2000) Biophys. J. , vol.78 , pp. 2163-2169
    • Kiihne, S.1    Bryant, R.G.2
  • 12
    • 0029129920 scopus 로고
    • Classes of hydration sites at protein-water interfaces: The source of contrast in magnetic resonance imaging
    • Koenig, S. H. 1995. Classes of hydration sites at protein-water interfaces: The source of contrast in magnetic resonance imaging. Biophys. J. 69:593-603.
    • (1995) Biophys. J. , vol.69 , pp. 593-603
    • Koenig, S.H.1
  • 13
    • 0027457662 scopus 로고
    • A unified view of relaxation in protein solutions and tissue including hydration and magnetization transfer
    • Koenig, S. H., R. D. I. Brown, and R. Ugolini. 1993. A unified view of relaxation in protein solutions and tissue including hydration and magnetization transfer. Magn. Reson. Med. 29:77-83.
    • (1993) Magn. Reson. Med. , vol.29 , pp. 77-83
    • Koenig, S.H.1    Brown, R.D.I.2    Ugolini, R.3
  • 14
    • 0000807992 scopus 로고
    • Protein-water interactions studied by solvent proton, deuteron, and oxygen-17 magnetic relaxation
    • Koenig, S. H., K. Hallenga, and M. Shporer. 1975. Protein-water interactions studied by solvent proton, deuteron, and oxygen-17 magnetic relaxation. Proc. Natl. Acad. Sci. USA. 72:2667-2671.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 2667-2671
    • Koenig, S.H.1    Hallenga, K.2    Shporer, M.3
  • 15
    • 0014690573 scopus 로고
    • Nuclear magnetic relaxation dispersion in protein solutions. I. Apotransferrin
    • Koenig, S. H., and W. E. Schillinger. 1969. Nuclear magnetic relaxation dispersion in protein solutions. I. Apotransferrin. J. Biol. Chem. 244:3283-3289.
    • (1969) J. Biol. Chem. , vol.244 , pp. 3283-3289
    • Koenig, S.H.1    Schillinger, W.E.2
  • 16
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B., and F. M. Richards. 1971. The interpretation of protein structures: Estimation of static accessibility. J. Mol. Biol. 55:379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 17
    • 0023051843 scopus 로고
    • Internal cavities and buried waters in globular proteins
    • Rashlin, A. A., M. Iofin, and B. Honig. 1986. Internal cavities and buried waters in globular proteins. Biochemistry. 25:3619-3625.
    • (1986) Biochemistry , vol.25 , pp. 3619-3625
    • Rashlin, A.A.1    Iofin, M.2    Honig, B.3
  • 18
    • 0017429069 scopus 로고
    • Areas, volumes, packing and protein structure
    • Richards, F. M. 1977. Areas, volumes, packing and protein structure. Annu. Rev. Biophys. Bioeng. 6:151-176.
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 19
    • 0033185778 scopus 로고    scopus 로고
    • Magnetic relaxation dispersion measurements of solute spin probes using a dual magnet system
    • Wagner, S., T. J. R. Dinesen, T. Rayner, and R. G. Bryant. 1999. Magnetic relaxation dispersion measurements of solute spin probes using a dual magnet system. J. Magn. Reson. 140:172-178.
    • (1999) J. Magn. Reson. , vol.140 , pp. 172-178
    • Wagner, S.1    Dinesen, T.J.R.2    Rayner, T.3    Bryant, R.G.4
  • 20
    • 0024291642 scopus 로고
    • Structure of phosphate free ribonuclease A refined to 1.26 A
    • Wlodawer, A., L. A. Svensson, L. Sjoln, and G. L. Gilleeland. 1988. Structure of phosphate free ribonuclease A refined to 1.26 A. Biochemistry. 27:2705-2727.
    • (1988) Biochemistry , vol.27 , pp. 2705-2727
    • Wlodawer, A.1    Svensson, L.A.2    Sjoln, L.3    Gilleeland, G.L.4
  • 21
    • 0014829630 scopus 로고
    • Segmental flexibility in an antibody molecule
    • Yguerabide, J., H. Epstein, and L. Stryer. 1970. Segmental flexibility in an antibody molecule. J. Mol. Biol. 51:573-590.
    • (1970) J. Mol. Biol. , vol.51 , pp. 573-590
    • Yguerabide, J.1    Epstein, H.2    Stryer, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.