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Volumn 7, Issue 9, 1999, Pages 1047-1055

Flap opening and dimer-interface flexibility in the free and inhibitor- bound HIV protease, and their implications for function

Author keywords

Chemical exchange; Dynamics; NMR; Protein; Relaxation

Indexed keywords

PROTEINASE;

EID: 0033200247     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80172-5     Document Type: Article
Times cited : (250)

References (55)
  • 2
    • 0032537169 scopus 로고    scopus 로고
    • Increasing survival in AIDS patients with cytomegalovirus retinitis treated with combination antiretroviral therapy including HIV protease inhibitors
    • 2. Walsh, J.C., Jones, C.D., Barnes, E.A., Gazzard, B.G. & Mitchell, S.M. (1998). Increasing survival in AIDS patients with cytomegalovirus retinitis treated with combination antiretroviral therapy including HIV protease inhibitors. AIDS 12, 613-618.
    • (1998) AIDS , vol.12 , pp. 613-618
    • Walsh, J.C.1    Jones, C.D.2    Barnes, E.A.3    Gazzard, B.G.4    Mitchell, S.M.5
  • 3
    • 0031856659 scopus 로고    scopus 로고
    • Resistance to HIV protease inhibitors
    • 3. Condra, J. H. (1998). Resistance to HIV protease inhibitors. Haemophilia 4, 610-615.
    • (1998) Haemophilia , vol.4 , pp. 610-615
    • Condra, J.H.1
  • 4
    • 0025336093 scopus 로고
    • Comparison of the crystal structures and intersubunit interactions of human immunodeficiency and Rous sarcoma virus proteases
    • 4. Weber, I.T. (1990). Comparison of the crystal structures and intersubunit interactions of human immunodeficiency and Rous sarcoma virus proteases. J. Biol. Chem. 265, 10492-10496.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10492-10496
    • Weber, I.T.1
  • 5
    • 0029775232 scopus 로고    scopus 로고
    • Crystal structures of complexes of a peptidic inhibitor with wild-type and two mutant HIV-1 proteases
    • 5. Hong, L., Treharne, A., Hartsuck, J.A., Foundling, S. & Tang, J. (1996). Crystal structures of complexes of a peptidic inhibitor with wild-type and two mutant HIV-1 proteases. Biochemistry 35, 10627-10633.
    • (1996) Biochemistry , vol.35 , pp. 10627-10633
    • Hong, L.1    Treharne, A.2    Hartsuck, J.A.3    Foundling, S.4    Tang, J.5
  • 6
    • 9544235162 scopus 로고    scopus 로고
    • Cyclic HIV protease inhibitors: Synthesis, conformational analysis, P2/P2′ structure-activity relationship, and molecular recognition of cyclic ureas
    • 6. Lam, P.Y., et al., & Hodge, C.N. (1996). Cyclic HIV protease inhibitors: synthesis, conformational analysis, P2/P2′ structure-activity relationship, and molecular recognition of cyclic ureas. J. Med. Chem. 39, 3514-3525.
    • (1996) J. Med. Chem. , vol.39 , pp. 3514-3525
    • Lam, P.Y.1    Hodge, C.N.2
  • 8
    • 0032562224 scopus 로고    scopus 로고
    • Domain flexibility in retroviral proteases: Structural implications for drug resistant mutations
    • 8. Rose, R.B., Craik, C.S. & Stroud, R.M. (1998). Domain flexibility in retroviral proteases: structural implications for drug resistant mutations. Biochemistry 37, 2607-2621.
    • (1998) Biochemistry , vol.37 , pp. 2607-2621
    • Rose, R.B.1    Craik, C.S.2    Stroud, R.M.3
  • 9
    • 0030598997 scopus 로고    scopus 로고
    • A combined quantum/classical molecular dynamics study of the catalytic mechanism of HIV protease
    • 9. Liu, H., Muller-Plathe, F. & van Gunsteren, W.F. (1996). A combined quantum/classical molecular dynamics study of the catalytic mechanism of HIV protease. J. Mol. Biol. 261, 454-469.
    • (1996) J. Mol. Biol. , vol.261 , pp. 454-469
    • Liu, H.1    Muller-Plathe, F.2    Van Gunsteren, W.F.3
  • 11
    • 0027468137 scopus 로고
    • Molecular dynamics simulation of HIV-1 protease in a crystalline environment and in solution
    • 11. York, D.M., Darden, T.A., Pedersen, L.G. & Anderson, M.W. (1993). Molecular dynamics simulation of HIV-1 protease in a crystalline environment and in solution. Biochemistry 32, 1443-1453.
    • (1993) Biochemistry , vol.32 , pp. 1443-1453
    • York, D.M.1    Darden, T.A.2    Pedersen, L.G.3    Anderson, M.W.4
  • 12
    • 0028958868 scopus 로고
    • Flap opening in HIV-1 protease simulated by 'activated' molecular dynamics
    • 12. Collins, J.R., Burt, S.K. & Erickson, J.W. (1995). Flap opening in HIV-1 protease simulated by 'activated' molecular dynamics. Nat. Struct. Biol. 2, 334-338.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 334-338
    • Collins, J.R.1    Burt, S.K.2    Erickson, J.W.3
  • 13
    • 0032127391 scopus 로고    scopus 로고
    • Reaction path and free energy calculations of the transition between alternate conformations of the HIV-1 protease
    • 13. Rick, S.W., Erickson, J.W. & Burt, S.K. (1998). Reaction path and free energy calculations of the transition between alternate conformations of the HIV-1 protease. Proteins 32, 7-16.
    • (1998) Proteins , vol.32 , pp. 7-16
    • Rick, S.W.1    Erickson, J.W.2    Burt, S.K.3
  • 15
    • 0027309442 scopus 로고
    • Inhibitor binding to the Phe53Trp mutant of HIV-1 protease promotes conformational changes detectable by spectrofluorometry
    • 15. Rodriguez, E.J., Debouck, C., Deckman, I.C., Abu-Soud, H., Raushel, F.M. & Meek, T.D. (1993). Inhibitor binding to the Phe53Trp mutant of HIV-1 protease promotes conformational changes detectable by spectrofluorometry. Biochemistry 32, 3557-3563.
    • (1993) Biochemistry , vol.32 , pp. 3557-3563
    • Rodriguez, E.J.1    Debouck, C.2    Deckman, I.C.3    Abu-Soud, H.4    Raushel, F.M.5    Meek, T.D.6
  • 16
    • 0032574705 scopus 로고    scopus 로고
    • Molecular basis of resistance to HIV-1 protease inhibition: A plausible hypothesis
    • 16. Luque, I., Todd, M.J., Gomez, J., Semo, N. & Freire, E. (1998). Molecular basis of resistance to HIV-1 protease inhibition: a plausible hypothesis. Biochemistry 37, 5791-5797.
    • (1998) Biochemistry , vol.37 , pp. 5791-5797
    • Luque, I.1    Todd, M.J.2    Gomez, J.3    Semo, N.4    Freire, E.5
  • 17
    • 0028921302 scopus 로고
    • Flexibility and function in HIV-1 protease
    • 17. Nicholson, L.K., et al., & Jadhav, P.K. (1995). Flexibility and function in HIV-1 protease. Nat. Struct. Biol. 2, 274-280.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 274-280
    • Nicholson, L.K.1    Jadhav, P.K.2
  • 18
    • 0032511368 scopus 로고    scopus 로고
    • Flexibility and function in HIV protease - Dynamics of the HIV-1 protease bound to the asymmetric Inhibitor kynostatin 272 (KNI-272)
    • 18. Freedberg, D.I., et al., & Torchia, D.A. (1998). Flexibility and function in HIV protease - dynamics of the HIV-1 protease bound to the asymmetric Inhibitor kynostatin 272 (KNI-272). J. Am, Chem. Soc. 120, 7916-7923.
    • (1998) J. Am, Chem. Soc. , vol.120 , pp. 7916-7923
    • Freedberg, D.I.1    Torchia, D.A.2
  • 19
    • 0028105957 scopus 로고
    • The HIV-1 protease as enzyme and substrate: Mutagenesis of autolysis sites and generation of a stable mutant with retained kinetic properties
    • 19. Mildner, A.M., et al., & Tomasselli, A.G. (1994). The HIV-1 protease as enzyme and substrate: mutagenesis of autolysis sites and generation of a stable mutant with retained kinetic properties. Biochemistry 33, 9405-9413.
    • (1994) Biochemistry , vol.33 , pp. 9405-9413
    • Mildner, A.M.1    Tomasselli, A.G.2
  • 20
    • 0029913459 scopus 로고    scopus 로고
    • Conformational stability and catalytic activity of HIV-1 protease are both enhanced at high salt concentration
    • 20. Szeltner, Z. & Polgar, L. (1996). Conformational stability and catalytic activity of HIV-1 protease are both enhanced at high salt concentration. J. Biol. Chem. 271, 5458-5463.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5458-5463
    • Szeltner, Z.1    Polgar, L.2
  • 21
    • 0001144784 scopus 로고    scopus 로고
    • Monitoring macromolecular motions on microsecond-millisecond timescales by R1rho-R1 constant-relaxation-time NMR spectroscopy
    • 21. Akke, M. & Palmer, A.G. (1996). Monitoring macromolecular motions on microsecond-millisecond timescales by R1rho-R1 constant-relaxation-time NMR spectroscopy. J. Am. Chem. Soc. 118, 911-912.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 911-912
    • Akke, M.1    Palmer, A.G.2
  • 22
    • 0033003378 scopus 로고    scopus 로고
    • Microsecond timescale dynamics in RXR DNA binding domain from a combination of spin-echo and off-resonance rotating frame relaxation measurements
    • 22. Mulder, F.A.A., van Tilborg, P.J.A., Kaptein, R. & Boelens, R. (1998). Microsecond timescale dynamics in RXR DNA binding domain from a combination of spin-echo and off-resonance rotating frame relaxation measurements. J Biomol. NMR 13, 275-288.
    • (1998) J Biomol. NMR , vol.13 , pp. 275-288
    • Mulder, F.A.A.1    Van Tilborg, P.J.A.2    Kaptein, R.3    Boelens, R.4
  • 23
    • 0032517325 scopus 로고    scopus 로고
    • Using amide 1H and 15N transverse relaxation to detect millisecond time-scale motions in perdeuterated proteins: Application to HIV-1 protease
    • 23. Ishima, R., Wingfield, P.T., Stahl, S.J., Kaufman, J.D. & Torchia, D.A. (1998). Using amide 1H and 15N transverse relaxation to detect millisecond time-scale motions in perdeuterated proteins: application to HIV-1 protease. J. Am. Chem. Soc. 120, 10534-10542.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 10534-10542
    • Ishima, R.1    Wingfield, P.T.2    Stahl, S.J.3    Kaufman, J.D.4    Torchia, D.A.5
  • 24
    • 9044228016 scopus 로고    scopus 로고
    • Three-dimensional solution structure of the HIV-1 protease complexed with DMP323, a novel cyclic urea-type inhibitor, determined by nuclear magnetic resonance spectroscopy
    • 24. Yamazaki, T., et al., & Lam, P.Y. (1996). Three-dimensional solution structure of the HIV-1 protease complexed with DMP323, a novel cyclic urea-type inhibitor, determined by nuclear magnetic resonance spectroscopy. Protein Sci. 5, 495-506.
    • (1996) Protein Sci. , vol.5 , pp. 495-506
    • Yamazaki, T.1    Lam, P.Y.2
  • 25
    • 0027263501 scopus 로고
    • Regulation of autoproteolysis of the HIV-1 and HIV-2 proteases with engineered amino acid substitutions
    • 25. Rose, J.R., Salto, R. & Craik, C.S. (1993). Regulation of autoproteolysis of the HIV-1 and HIV-2 proteases with engineered amino acid substitutions. J. Biol. Chem. 268, 11939-11945.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11939-11945
    • Rose, J.R.1    Salto, R.2    Craik, C.S.3
  • 26
    • 0030066643 scopus 로고    scopus 로고
    • A transient precursor of the HIV-1 protease. Isolation, characterization, and kinetics of maturation
    • 26. Wondrak, E.M., Nashed, N.T., Haber, M.T., Jerina, D.M. & Louis, J.M. (1996). A transient precursor of the HIV-1 protease. Isolation, characterization, and kinetics of maturation. J. Biol. Chem. 271, 4477-4481.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4477-4481
    • Wondrak, E.M.1    Nashed, N.T.2    Haber, M.T.3    Jerina, D.M.4    Louis, J.M.5
  • 27
    • 0027936212 scopus 로고
    • Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyprotein
    • 27. Louis, J.M., Nashed, N.T., Parris, K.D., Kimmel, A.R. & Jerina, D.M. (1994). Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyprotein., Proc. Natl Acad. Sci. USA 91, 7970-7974.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 7970-7974
    • Louis, J.M.1    Nashed, N.T.2    Parris, K.D.3    Kimmel, A.R.4    Jerina, D.M.5
  • 28
    • 0032553427 scopus 로고
    • Characterization of human immunodeficiency virus type-1 (HIV-1) particles that express protease-reverse transcriptase fusion proteins
    • 28. Cherry, E., et al., & Wainberg, M.A. (1988). Characterization of human immunodeficiency virus type-1 (HIV-1) particles that express protease-reverse transcriptase fusion proteins. J. Mol. Biol. 284, 43-56.
    • (1988) J. Mol. Biol. , vol.284 , pp. 43-56
    • Cherry, E.1    Wainberg, M.A.2
  • 29
    • 20244373125 scopus 로고
    • X-ray analysis of HIV-1 proteinase at 2.7 A resolution confirms structural homology among retroviral enzymes
    • 29. Lapatto, R., et al., & Hobart, P.M. (1989). X-ray analysis of HIV-1 proteinase at 2.7 A resolution confirms structural homology among retroviral enzymes. Nature 342, 299-302.
    • (1989) Nature , vol.342 , pp. 299-302
    • Lapatto, R.1    Hobart, P.M.2
  • 30
    • 0024412506 scopus 로고
    • Conserved folding in retroviral proteases: Crystal structure of a synthetic HIV-1 protease
    • 30. Wlodawer, A., et al., & Kent, S.B. (1989). Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease. Science 245, 616-621.
    • (1989) Science , vol.245 , pp. 616-621
    • Wlodawer, A.1    Kent, S.B.2
  • 31
    • 0026344399 scopus 로고
    • The three-dimensional structure of the aspartyl protease from the HIV-1 isolate BRU
    • 31. Spinelli, S., Liu, Q.Z., Alzari, P.M., Hirel, P.H. & Poljak, R.J. (1991). The three-dimensional structure of the aspartyl protease from the HIV-1 isolate BRU. Biochimie 73, 1391-1396.
    • (1991) Biochimie , vol.73 , pp. 1391-1396
    • Spinelli, S.1    Liu, Q.Z.2    Alzari, P.M.3    Hirel, P.H.4    Poljak, R.J.5
  • 32
    • 0027943157 scopus 로고
    • Crystal structure at 1.9-A resolution of human immunodeficiency virus (HIV) II protease complexed with L-735,524, an orally bioavailable inhibitor of the HIV proteases
    • 32. Chen, Z., et al., & Kuo, L.C. (1994). Crystal structure at 1.9-A resolution of human immunodeficiency virus (HIV) II protease complexed with L-735,524, an orally bioavailable inhibitor of the HIV proteases. J. Biol. Chem. 269, 26344-26348.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26344-26348
    • Chen, Z.1    Kuo, L.C.2
  • 33
    • 0028927329 scopus 로고
    • Effect of point mutations on the kinetics and the inhibition of human immunodeficiency virus type 1 protease: Relationship to drug resistance
    • 33. Lin, Y., et al., & Tang, J. (1995). Effect of point mutations on the kinetics and the inhibition of human immunodeficiency virus type 1 protease: relationship to drug resistance. Biochemistry 34, 1143-1152.
    • (1995) Biochemistry , vol.34 , pp. 1143-1152
    • Lin, Y.1    Tang, J.2
  • 34
    • 0028911958 scopus 로고
    • A side chain at position 48 of the human immunodeficiency virus type-1 protease flap provides an additional specificity determinant
    • 34. Moody, M.D., et al., & Swanstrom, R. (1995). A side chain at position 48 of the human immunodeficiency virus type-1 protease flap provides an additional specificity determinant. Virology 207, 475-485.
    • (1995) Virology , vol.207 , pp. 475-485
    • Moody, M.D.1    Swanstrom, R.2
  • 35
    • 0030910583 scopus 로고    scopus 로고
    • Sequence requirements of the HIV-1 protease flap region determined by saturation mutagenesis and kinetic analysis of flap mutants
    • 35. Shao, W., Everitt, L., Manchester, M., Loeb, D.D., Hutchison, C.A. III & Swanstrom, R. (1997). Sequence requirements of the HIV-1 protease flap region determined by saturation mutagenesis and kinetic analysis of flap mutants., Proc. Natl Acad. Sci. USA 94, 2243-2248.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 2243-2248
    • Shao, W.1    Everitt, L.2    Manchester, M.3    Loeb, D.D.4    Hutchison C.A. III5    Swanstrom, R.6
  • 36
    • 0031042369 scopus 로고    scopus 로고
    • Activity of tethered human immunodeficiency virus 1 protease containing mutations in the flap region of one subunit
    • 36. Tozser, J., et al., & Oroszlan, S. (1997). Activity of tethered human immunodeficiency virus 1 protease containing mutations in the flap region of one subunit. Eur. J. Biochem. 244, 235-241.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 235-241
    • Tozser, J.1    Oroszlan, S.2
  • 37
    • 0029644939 scopus 로고
    • Structure of HIV-1 protease with KNI-272, a tight-binding transition-state analog containing allophenylnorstatine
    • 37. Baldwin, E.T., et al., & Erickson, J.W. (1995). Structure of HIV-1 protease with KNI-272, a tight-binding transition-state analog containing allophenylnorstatine. Structure 3, 581-590.
    • (1995) Structure , vol.3 , pp. 581-590
    • Baldwin, E.T.1    Erickson, J.W.2
  • 38
    • 0025823572 scopus 로고
    • On the role of methionine residues in the sequence-independent recognition of nonpolar protein surfaces
    • 38. Gellman, S.H. (1991). On the role of methionine residues in the sequence-independent recognition of nonpolar protein surfaces. Biochemistry 30, 6633-6636.
    • (1991) Biochemistry , vol.30 , pp. 6633-6636
    • Gellman, S.H.1
  • 39
    • 0030474628 scopus 로고    scopus 로고
    • Bound water molecules at the interface between the HIV-1 protease and a potent inhibitor, KNI-272, determined by NMR
    • 39. Wang, Y.X., et al., & Torchia, D.A. (1996). Bound water molecules at the interface between the HIV-1 protease and a potent inhibitor, KNI-272, determined by NMR. J. Am. Chem. Soc. 118, 12287-12290.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 12287-12290
    • Wang, Y.X.1    Torchia, D.A.2
  • 40
    • 0029833678 scopus 로고    scopus 로고
    • Influence of flanking sequences on the dimer stability of human immunodeficiency virus type 1 protease
    • 40. Wondrak, E.M. & Louis, J.M. (1996). Influence of flanking sequences on the dimer stability of human immunodeficiency virus type 1 protease. Biochemistry 35, 12957-12962.
    • (1996) Biochemistry , vol.35 , pp. 12957-12962
    • Wondrak, E.M.1    Louis, J.M.2
  • 41
    • 0030669385 scopus 로고    scopus 로고
    • Crystallographic analysis of human immunodeficiency virus 1 protease with an analog of the conserved CA-p2 substrate-interactions with frequently occurring glutamic acid residue at P2′ position of substrates
    • 41. Weber, I.T., et al., & Louis, J.M. (1997). Crystallographic analysis of human immunodeficiency virus 1 protease with an analog of the conserved CA-p2 substrate-interactions with frequently occurring glutamic acid residue at P2′ position of substrates. Eur. J. Biochem. 249, 523-530.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 523-530
    • Weber, I.T.1    Louis, J.M.2
  • 42
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • 42. Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J. & Bax, A. (1995). NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 43
    • 0028472289 scopus 로고
    • Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1rho and T2(CPMG) methods
    • 43. Davis, D.G., Perlman, M.E. & London, R.E. (1994). Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1rho and T2(CPMG) methods. J. Magn. Reson. B 104, 266-275.
    • (1994) J. Magn. Reson. B , vol.104 , pp. 266-275
    • Davis, D.G.1    Perlman, M.E.2    London, R.E.3
  • 44
    • 0000698894 scopus 로고    scopus 로고
    • Systematic errors associated with the CPMG pulse sequence and their effect on motional analysis of biomolecules
    • 44. Ross, A., Czisch, M. & King, G.C. (1997). Systematic errors associated with the CPMG pulse sequence and their effect on motional analysis of biomolecules. J. Magn. Reson. 124, 355-365.
    • (1997) J. Magn. Reson. , vol.124 , pp. 355-365
    • Ross, A.1    Czisch, M.2    King, G.C.3
  • 45
    • 36849127400 scopus 로고
    • Nuclear magnetic resonance study of the protolysis of trimethylammonium ion in aqueous solution - Order of the reaction with respect to solvent
    • 45. Luz, Z. & Meiboom, S. (1963). Nuclear magnetic resonance study of the protolysis of trimethylammonium ion in aqueous solution - order of the reaction with respect to solvent. J. Chem. Phys. 39, 366-370.
    • (1963) J. Chem. Phys. , vol.39 , pp. 366-370
    • Luz, Z.1    Meiboom, S.2
  • 46
    • 48549112585 scopus 로고
    • Interference effects in the relaxation of a pair of unlike spin-1/2 nuclei
    • 46. Goldman, M. (1984). Interference effects in the relaxation of a pair of unlike spin-1/2 nuclei. J. Magn. Reson. 60, 437-452.
    • (1984) J. Magn. Reson. , vol.60 , pp. 437-452
    • Goldman, M.1
  • 48
    • 0000555643 scopus 로고
    • Spin-echo studies of chemical exchange. II. Closed formulas for two sites
    • 48. Allerhand, A. & Gutowsky, H.S. (1965). Spin-echo studies of chemical exchange. II. Closed formulas for two sites. J. Chem. Phys. 42, 1587-1598.
    • (1965) J. Chem. Phys. , vol.42 , pp. 1587-1598
    • Allerhand, A.1    Gutowsky, H.S.2
  • 49
    • 36849140579 scopus 로고
    • Spin echoes and chemical exchange
    • 49. Bloom, M., Reeves, L.W. & Wells, E.J. (1965). Spin echoes and chemical exchange. J. Chem. Phys. 42, 1615-1624.
    • (1965) J. Chem. Phys. , vol.42 , pp. 1615-1624
    • Bloom, M.1    Reeves, L.W.2    Wells, E.J.3
  • 50
    • 0002889918 scopus 로고
    • A general two-site solution for the chemical exchange produced dependence of T2 upon Carr-Purcell pulse separation
    • 50. Carver, J.P. & Richards, R.E. (1972). A general two-site solution for the chemical exchange produced dependence of T2 upon Carr-Purcell pulse separation. J. Magn. Reson. 6, 89-105.
    • (1972) J. Magn. Reson. , vol.6 , pp. 89-105
    • Carver, J.P.1    Richards, R.E.2
  • 51
    • 0030445011 scopus 로고    scopus 로고
    • Dynamics of ribonuclease H: Temperature dependence of motions on multiple timescales
    • 51. Mandel, A.M., Akke, M. & Palmer, A.G. III (1996). Dynamics of ribonuclease H: temperature dependence of motions on multiple timescales. Biochemistry 35, 16009-16023.
    • (1996) Biochemistry , vol.35 , pp. 16009-16023
    • Mandel, A.M.1    Akke, M.2    Palmer A.G. III3
  • 52
    • 0028541223 scopus 로고
    • A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization
    • 52. Schurr, J.M., Babcock, H.P. & Fujimoto, B.S. (1994). A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization. J. Magn. Reson. B 105, 211-224
    • (1994) J. Magn. Reson. B , vol.105 , pp. 211-224
    • Schurr, J.M.1    Babcock, H.P.2    Fujimoto, B.S.3
  • 53
    • 0031591390 scopus 로고    scopus 로고
    • Enhanced protein flexibility caused by a destabilizing amino acid replacement in BPTI
    • 53. Beeser, S.A., Goldenburg, D.P. & Oas, T.G. (1997). Enhanced protein flexibility caused by a destabilizing amino acid replacement in BPTI. J. Mol. Biol. 269, 154-164.
    • (1997) J. Mol. Biol. , vol.269 , pp. 154-164
    • Beeser, S.A.1    Goldenburg, D.P.2    Oas, T.G.3
  • 54
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • 54. Wishart, D.S., Sykes, B.D. & Richards, F.M. (1991). Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222, 311-333.
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 55
    • 0031237104 scopus 로고    scopus 로고
    • Chemical shift tensors in peptides: A quantum mechanical study
    • 55. Walling, A.E., Pargas, R.E. & de Dios, A.C. (1997). Chemical shift tensors in peptides: a quantum mechanical study. J. Phys. Chem. A 101, 7299-7303.
    • (1997) J. Phys. Chem. A , vol.101 , pp. 7299-7303
    • Walling, A.E.1    Pargas, R.E.2    De Dios, A.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.