메뉴 건너뛰기




Volumn 166, Issue 2, 2004, Pages 190-201

Amide proton relaxation measurements employing a highly deuterated protein

Author keywords

Cross relaxation; Deuteration; Protein dynamics; Proton relaxation; Spin diffusion

Indexed keywords

ANISOTROPY; COMPUTER SIMULATION; DIFFUSION; MAGNETIZATION; MOLECULAR STRUCTURE; PLASTICITY; PROTEINS; SOLVENTS;

EID: 0346969535     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmr.2003.10.012     Document Type: Article
Times cited : (17)

References (56)
  • 2
    • 0034753415 scopus 로고    scopus 로고
    • Solution structure of Ca2+-calmodulin reveals flexible hand-like properties of its domains
    • Chou J.J., Li S.P., Klee C.B., Bax A. Solution structure of Ca2+-calmodulin reveals flexible hand-like properties of its domains. Nat. Struct. Biol. 8:2001;990-997.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 990-997
    • Chou, J.J.1    Li, S.P.2    Klee, C.B.3    Bax, A.4
  • 3
    • 0034760077 scopus 로고    scopus 로고
    • Dynamic activation of protein function: A view emerging from NMR spectroscopy
    • Wand A.J. Dynamic activation of protein function: a view emerging from NMR spectroscopy. Nat. Struct. Biol. 8:2001;926-931.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 926-931
    • Wand, A.J.1
  • 4
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules
    • Palmer A.G., Kroenke C.D., Loria J.P. Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Methods Enzymol. 339:2001;204-238.
    • (2001) Methods Enzymol. , vol.339 , pp. 204-238
    • Palmer, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 6
    • 0031853060 scopus 로고    scopus 로고
    • Protein dynamics from NMR
    • Kay L.E. Protein dynamics from NMR. Nat. Struct. Biol. 5:1998;513-517.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 513-517
    • Kay, L.E.1
  • 7
    • 0024449503 scopus 로고
    • Backbone dynamics of proteins as studied by N-15 inverse detected heteronuclear nmr-spectroscopy - Application to staphylococcal nuclease
    • Kay L.E., Torchia D.A., Bax A. Backbone dynamics of proteins as studied by N-15 inverse detected heteronuclear nmr-spectroscopy - application to staphylococcal nuclease. Biochemistry. 28:1989;8972-8979.
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 8
    • 0000386638 scopus 로고
    • Proton magnetic relaxation and spin diffusion in proteins
    • Kalk A., Berendsen H.J.C. Proton magnetic relaxation and spin diffusion in proteins. J. Magn. Reson. 24:1976;343-366.
    • (1976) J. Magn. Reson. , vol.24 , pp. 343-366
    • Kalk, A.1    Berendsen, H.J.C.2
  • 9
    • 0037024180 scopus 로고    scopus 로고
    • Deuterium spin probes of side-chain dynamics in proteins. 1. Measurement of five relaxation rates per deuteron in C-13-labeled and fractionally H-2-enriched proteins in solution
    • Millet O., Muhandiram D.R., Skrynnikov N.R., Kay L.E. Deuterium spin probes of side-chain dynamics in proteins. 1. Measurement of five relaxation rates per deuteron in C-13-labeled and fractionally H-2-enriched proteins in solution. J. Am. Chem. Soc. 124:2002;6439-6448.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 6439-6448
    • Millet, O.1    Muhandiram, D.R.2    Skrynnikov, N.R.3    Kay, L.E.4
  • 10
    • 0037024197 scopus 로고    scopus 로고
    • Deuterium spin probes of side-chain dynamics in proteins. 2. Spectral density mapping and identification of nanosecond time-scale side-chain motions
    • Skrynnikov N.R., Millet O., Kay L.E. Deuterium spin probes of side-chain dynamics in proteins. 2. Spectral density mapping and identification of nanosecond time-scale side-chain motions. J. Am. Chem. Soc. 124:2002;6449-6460.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 6449-6460
    • Skrynnikov, N.R.1    Millet, O.2    Kay, L.E.3
  • 11
    • 0014427626 scopus 로고
    • Proton magnetic resonance of proteins fully deuterated except for 1 H-Leucine side chains
    • Crespi H.L., Rosenberg R.M., Katz J.J. Proton magnetic resonance of proteins fully deuterated except for 1 H-Leucine side chains. Science. 161:1968;795-796.
    • (1968) Science , vol.161 , pp. 795-796
    • Crespi, H.L.1    Rosenberg, R.M.2    Katz, J.J.3
  • 12
    • 0014424848 scopus 로고
    • High-resolution nuclear magnetic resonance spectra of selectively deuterated staphylococcal nuclease
    • Markley J.L., Putter I., Jardetzky O. High-resolution nuclear magnetic resonance spectra of selectively deuterated staphylococcal nuclease. Science. 161:1968;1249-1251.
    • (1968) Science , vol.161 , pp. 1249-1251
    • Markley, J.L.1    Putter, I.2    Jardetzky, O.3
  • 13
    • 0346967484 scopus 로고
    • Utilization of selective deuteration in Nmr spectral assignment of deoxyoligonucleotides - 2d noesy analysis of non-self - Complementary duplexes
    • Brush C.K., Stone M.P., Harris T.M. Utilization of selective deuteration in Nmr spectral assignment of deoxyoligonucleotides - 2d noesy analysis of non-self - complementary duplexes. Biochemistry. 26:1987;4164-4164.
    • (1987) Biochemistry , vol.26 , pp. 4164-4164
    • Brush, C.K.1    Stone, M.P.2    Harris, T.M.3
  • 15
    • 0030849954 scopus 로고    scopus 로고
    • Conformation of the principal neutralizing determinant of human immunodeficiency virus type 1 in complex with an anti-gp120 virus neutralizing antibody studied by two-dimensional nuclear magnetic resonance difference spectroscopy
    • Zvi A., Feigelson D.J., Hayek Y., Anglister J. Conformation of the principal neutralizing determinant of human immunodeficiency virus type 1 in complex with an anti-gp120 virus neutralizing antibody studied by two-dimensional nuclear magnetic resonance difference spectroscopy. Biochemistry. 36:1997;8619-8627.
    • (1997) Biochemistry , vol.36 , pp. 8619-8627
    • Zvi, A.1    Feigelson, D.J.2    Hayek, Y.3    Anglister, J.4
  • 16
    • 0037354160 scopus 로고    scopus 로고
    • A sensitive and robust method for obtaining intermolecular NOEs between side chains in large protein complexes
    • Gross J.D., Gelev V.M., Wagner G. A sensitive and robust method for obtaining intermolecular NOEs between side chains in large protein complexes. J. Biomol. NMR. 25:2003;235-242.
    • (2003) J. Biomol. NMR , vol.25 , pp. 235-242
    • Gross, J.D.1    Gelev, V.M.2    Wagner, G.3
  • 17
    • 0028119538 scopus 로고
    • An HNCA pulse scheme for the backbone assignment of N-15,C-13, H-2-labeled proteins - Application to a 37-kDa TRP Repressor DNA complex
    • Yamazaki T., Lee W., Revington M., Mattiello D.L., Dahlquist F.W., Arrowsmith C.H., Kay L.E. An HNCA pulse scheme for the backbone assignment of N-15,C-13,H-2-labeled proteins - application to a 37-kDa TRP Repressor DNA complex. J. Am. Chem. Soc. 116:1994;6464-6465.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 6464-6465
    • Yamazaki, T.1    Lee, W.2    Revington, M.3    Mattiello, D.L.4    Dahlquist, F.W.5    Arrowsmith, C.H.6    Kay, L.E.7
  • 19
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T-2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • Pervushin K., Riek R., Wider G., Wuthrich K. Attenuated T-2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc. Natl. Acad. Sci. USA. 94:1997;12366-12371.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wuthrich, K.4
  • 20
    • 0032517325 scopus 로고    scopus 로고
    • Using amide H-1 and N-15 transverse relaxation to detect millisecond time-scale motions in perdeuterated proteins: Application to HIV-1 protease
    • Ishima R., Wingfield P.T., Stahl S.J., Kaufman J.D., Torchia D.A. Using amide H-1 and N-15 transverse relaxation to detect millisecond time-scale motions in perdeuterated proteins: application to HIV-1 protease. J. Am. Chem. Soc. 120:1998;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
  • 22
    • 0032133387 scopus 로고    scopus 로고
    • Some NMR experiments and a structure determination employing a N-15,H-2 enriched protein
    • Mal T.K., Matthews S.J., Kovacs H., Campbell I.D., Boyd J. Some NMR experiments and a structure determination employing a N-15,H-2 enriched protein. J. Biomol. NMR. 12:1998;259-276.
    • (1998) J. Biomol. NMR , vol.12 , pp. 259-276
    • Mal, T.K.1    Matthews, S.J.2    Kovacs, H.3    Campbell, I.D.4    Boyd, J.5
  • 23
    • 0032162217 scopus 로고    scopus 로고
    • Effect of deuteration on the accuracy of HN-HN distance constraints
    • Briercheck D.M., Rule G.S. Effect of deuteration on the accuracy of HN-HN distance constraints. J. Magn. Reson. 134:1998;52-56.
    • (1998) J. Magn. Reson. , vol.134 , pp. 52-56
    • Briercheck, D.M.1    Rule, G.S.2
  • 24
    • 0026834614 scopus 로고
    • The effect of selective deuteration on magnetization transfer in larger proteins
    • Pachter R., Arrowsmith C.H., Jardetzky O. The effect of selective deuteration on magnetization transfer in larger proteins. J. Biomol. NMR. 2:1992;183-194.
    • (1992) J. Biomol. NMR , vol.2 , pp. 183-194
    • Pachter, R.1    Arrowsmith, C.H.2    Jardetzky, O.3
  • 25
    • 0033654959 scopus 로고    scopus 로고
    • Preparation of isotopically labeled recombinant fragments of fibronectin for functional and structural study by heteronuclear nuclear magnetic resonance spectroscopy
    • Bright J.R., Pickford A.R., Potts J.R., Campbell I.D. Preparation of isotopically labeled recombinant fragments of fibronectin for functional and structural study by heteronuclear nuclear magnetic resonance spectroscopy. Methods Mol. Biol. 139:2000;59-69.
    • (2000) Methods Mol. Biol. , vol.139 , pp. 59-69
    • Bright, J.R.1    Pickford, A.R.2    Potts, J.R.3    Campbell, I.D.4
  • 26
    • 0032512876 scopus 로고    scopus 로고
    • Solution structure of the glycosylated second type 2 module of fibronectin
    • Sticht H., Pickford A.R., Potts J.R., Campbell I.D. Solution structure of the glycosylated second type 2 module of fibronectin. J. Mol. Biol. 276:1998;177-187.
    • (1998) J. Mol. Biol. , vol.276 , pp. 177-187
    • Sticht, H.1    Pickford, A.R.2    Potts, J.R.3    Campbell, I.D.4
  • 28
    • 0036390058 scopus 로고    scopus 로고
    • The effects of dissolved oxygen upon amide proton relaxation and chemical shift in a perdeuterated protein
    • Ulmer T.S., Campbell I.D., Boyd J. The effects of dissolved oxygen upon amide proton relaxation and chemical shift in a perdeuterated protein. J. Magn. Reson. 157:2002;181-189.
    • (2002) J. Magn. Reson. , vol.157 , pp. 181-189
    • Ulmer, T.S.1    Campbell, I.D.2    Boyd, J.3
  • 29
    • 0001070626 scopus 로고
    • Fourier transform study of NMR spin-lattice relaxation by progressive saturation
    • Freeman R., Hill H.D.W. Fourier transform study of NMR spin-lattice relaxation by progressive saturation. J. Chem. Phys. 54:1971;3367-3377.
    • (1971) J. Chem. Phys. , vol.54 , pp. 3367-3377
    • Freeman, R.1    Hill, H.D.W.2
  • 31
    • 58149363306 scopus 로고
    • Suppression of radiation damping in multidimensional Nmr experiments using magnetic-field gradients
    • Sklenar V. Suppression of radiation damping in multidimensional Nmr experiments using magnetic-field gradients. J. Magn. Reson. Ser. A. 114:1995;132-135.
    • (1995) J. Magn. Reson. Ser. A , vol.114 , pp. 132-135
    • Sklenar, V.1
  • 32
    • 44049118502 scopus 로고
    • Pulse sequences for removal of the effects of cross-correlation between dipolar and chemical-shift anisotropy relaxation mechanism on the measurement of heteronuclear T1 and T2 values in proteins
    • Kay L.E., Nicholson L.K., Delaglio F., Bax A., Torchia D.A. Pulse sequences for removal of the effects of cross-correlation between dipolar and chemical-shift anisotropy relaxation mechanism on the measurement of heteronuclear T1 and T2 values in proteins. J. Magn. Reson. 97:1992;359-375.
    • (1992) J. Magn. Reson. , vol.97 , pp. 359-375
    • Kay, L.E.1    Nicholson, L.K.2    Delaglio, F.3    Bax, A.4    Torchia, D.A.5
  • 33
    • 0001484114 scopus 로고
    • Influence of cross-correlation between dipolar and anisotropic chemical-shift relaxation mechanisms upon longitudinal relaxation rates of N-15 in macromolecules
    • Boyd J., Hommel U., Campbell I.D. Influence of cross-correlation between dipolar and anisotropic chemical-shift relaxation mechanisms upon longitudinal relaxation rates of N-15 in macromolecules. Chem. Phys. Lett. 175:1990;477-482.
    • (1990) Chem. Phys. Lett. , vol.175 , pp. 477-482
    • Boyd, J.1    Hommel, U.2    Campbell, I.D.3
  • 34
    • 13444269041 scopus 로고
    • Computer-optimized decoupling scheme for wideband applications and low-level operation
    • Shaka A.J., Barker P.B., Freeman R. Computer-optimized decoupling scheme for wideband applications and low-level operation. J. Magn. Reson. 64:1985;547-552.
    • (1985) J. Magn. Reson. , vol.64 , pp. 547-552
    • Shaka, A.J.1    Barker, P.B.2    Freeman, R.3
  • 35
    • 0000486802 scopus 로고
    • Suppression of the effects of cross-correlation between dipolar and anisotropic chemical-shift relaxation mechanisms in the measurement of spin spin relaxation rates
    • Palmer A.G., Skelton N.J., Chazin W.J., Wright P.E., Rance M. Suppression of the effects of cross-correlation between dipolar and anisotropic chemical-shift relaxation mechanisms in the measurement of spin spin relaxation rates. Mol. Phys. 75:1992;699-711.
    • (1992) Mol. Phys. , vol.75 , pp. 699-711
    • Palmer, A.G.1    Skelton, N.J.2    Chazin, W.J.3    Wright, P.E.4    Rance, M.5
  • 36
    • 0033090632 scopus 로고    scopus 로고
    • Detection of intermolecular chemical exchange through decorrelation of two-spin order
    • Skrynnikov N.R., Ernst R.R. Detection of intermolecular chemical exchange through decorrelation of two-spin order. J. Magn. Reson. 137:1999;276-280.
    • (1999) J. Magn. Reson. , vol.137 , pp. 276-280
    • Skrynnikov, N.R.1    Ernst, R.R.2
  • 37
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 1. theory and range of validity
    • Lipari G., Szabo A. Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 1. theory and range of validity. J. Am. Chem. Soc. 104:1982;4546-4559.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 38
    • 0032477283 scopus 로고    scopus 로고
    • ′, and C(alpha)-H-alpha effective bond lengths in a protein by NMR in a dilute liquid crystalline phase
    • ′, and C(alpha)-H-alpha effective bond lengths in a protein by NMR in a dilute liquid crystalline phase J. Am. Chem. Soc. 120:1998;12334-12341.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 12334-12341
    • Ottiger, M.1    Bax, A.2
  • 39
    • 0033581191 scopus 로고    scopus 로고
    • Characterization of N-15 chemical shift anisotropy from orientation-dependent changes to N-15 chemical shifts in dilute bicelle solutions
    • Boyd J., Redfield C. Characterization of N-15 chemical shift anisotropy from orientation-dependent changes to N-15 chemical shifts in dilute bicelle solutions. J. Am. Chem. Soc. 121:1999;7441-7442.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 7441-7442
    • Boyd, J.1    Redfield, C.2
  • 40
    • 0034684181 scopus 로고    scopus 로고
    • Measurement of proton, nitrogen, and carbonyl chemical shielding anisotropies in a protein dissolved in a dilute liquid crystalline phase
    • Cornilescu G., Bax A. Measurement of proton, nitrogen, and carbonyl chemical shielding anisotropies in a protein dissolved in a dilute liquid crystalline phase. J. Am. Chem. Soc. 122:2000;10143-10154.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 10143-10154
    • Cornilescu, G.1    Bax, A.2
  • 41
    • 0032576119 scopus 로고    scopus 로고
    • Direct measurement of N-15 chemical shift anisotropy in solution
    • Fushman D., Tjandra N., Cowburn D. Direct measurement of N-15 chemical shift anisotropy in solution. J. Am. Chem. Soc. 120:1998;10947-10952.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 10947-10952
    • Fushman, D.1    Tjandra, N.2    Cowburn, D.3
  • 42
    • 36149008265 scopus 로고
    • Relaxation processes in a system of two spins
    • Solomon I. Relaxation processes in a system of two spins. Phys. Rev. 99:1955;559-565.
    • (1955) Phys. Rev. , vol.99 , pp. 559-565
    • Solomon, I.1
  • 43
    • 0034701315 scopus 로고    scopus 로고
    • Experimental measurement of nonuniform dioxygen accessibility to ribonuclease a surface and interior
    • Teng C.L., Bryant R.G. Experimental measurement of nonuniform dioxygen accessibility to ribonuclease a surface and interior. J. Am. Chem. Soc. 122:2000;2667-2668.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2667-2668
    • Teng, C.L.1    Bryant, R.G.2
  • 44
    • 0030797606 scopus 로고    scopus 로고
    • Application of phase-modulated CLEAN chemical EXchange spectroscopy (CLEANEX-PM) to detect water-protein proton exchange and intermolecular NOEs
    • Hwang T.L., Mori S., Shaka A.J., vanZijl P.C.M. Application of phase-modulated CLEAN chemical EXchange spectroscopy (CLEANEX-PM) to detect water-protein proton exchange and intermolecular NOEs. J. Am. Chem. Soc. 119:1997;6203-6204.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 6203-6204
    • Hwang, T.L.1    Mori, S.2    Shaka, A.J.3    Vanzijl, P.C.M.4
  • 45
    • 0030919951 scopus 로고    scopus 로고
    • Water H-1 magnetic relaxation dispersion in protein solutions. A quantitative assessment of internal hydration, proton exchange, and cross-relaxation
    • Venu K., Denisov V.P., Halle B. Water H-1 magnetic relaxation dispersion in protein solutions. A quantitative assessment of internal hydration, proton exchange, and cross-relaxation. J. Am. Chem. Soc. 119:1997;3122-3134.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 3122-3134
    • Venu, K.1    Denisov, V.P.2    Halle, B.3
  • 46
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen-exchange
    • Bai Y.W., Milne J.S., Mayne L., Englander S.W. Primary structure effects on peptide group hydrogen-exchange. Proteins. 17:1993;75-86.
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.W.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 47
    • 0037028967 scopus 로고    scopus 로고
    • Calculations of the contribution of ring currents to the chemical shielding anisotropy
    • Boyd J., Skrynnikov N.R. Calculations of the contribution of ring currents to the chemical shielding anisotropy. J. Am. Chem. Soc. 124:2002;1832-1833.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 1832-1833
    • Boyd, J.1    Skrynnikov, N.R.2
  • 48
    • 0001331889 scopus 로고    scopus 로고
    • Thermal offset viscosities of liquid H2O, D2O, and T2O
    • Cho C.H., Urquidi J., Singh S., Robinson G.W. Thermal offset viscosities of liquid H2O, D2O, and T2O. J. Phys. Chem. B. 103:1999;1991-1994.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 1991-1994
    • Cho, C.H.1    Urquidi, J.2    Singh, S.3    Robinson, G.W.4
  • 51
    • 0021754836 scopus 로고
    • Motional averaging of Proton nuclear overhauser effects in proteins - Predictions from a molecular-dynamics simulation of lysozyme
    • Olejniczak E.T., Dobson C.M., Karplus M., Levy R.M. Motional averaging of Proton nuclear overhauser effects in proteins - predictions from a molecular-dynamics simulation of lysozyme. J. Am. Chem. Soc. 106:1984;1923-1930.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 1923-1930
    • Olejniczak, E.T.1    Dobson, C.M.2    Karplus, M.3    Levy, R.M.4
  • 52
    • 0001767250 scopus 로고
    • Influence of rapid intramolecular motion on nmr cross-relaxation rates - A molecular-dynamics study of antamanide in solution
    • Bruschweiler R., Roux B., Blackledge M., Griesinger C., Karplus M., Ernst R.R. Influence of rapid intramolecular motion on nmr cross-relaxation rates - a molecular-dynamics study of antamanide in solution. J. Am. Chem. Soc. 114:1992;2289-2302.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 2289-2302
    • Bruschweiler, R.1    Roux, B.2    Blackledge, M.3    Griesinger, C.4    Karplus, M.5    Ernst, R.R.6
  • 53
    • 0029044470 scopus 로고
    • Nmr cross-relaxation investigated by molecular-dynamics simulation - A case-study of ubiquitin in solution
    • Abseher R., Ludemann S., Schreiber H., Steinhauser O. Nmr cross-relaxation investigated by molecular-dynamics simulation - a case-study of ubiquitin in solution. J. Mol. Biol. 249:1995;604-624.
    • (1995) J. Mol. Biol. , vol.249 , pp. 604-624
    • Abseher, R.1    Ludemann, S.2    Schreiber, H.3    Steinhauser, O.4
  • 54
    • 0000643959 scopus 로고    scopus 로고
    • Optimal sampling strategies for the measurement of relaxation times in proteins
    • Jones J.A. Optimal sampling strategies for the measurement of relaxation times in proteins. J. Magn. Reson. 126:1997;283-286.
    • (1997) J. Magn. Reson. , vol.126 , pp. 283-286
    • Jones, J.A.1
  • 55
    • 12044256620 scopus 로고
    • Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance C-12 heteronuclear Nmr-spectroscopy
    • Palmer A.G., Rance M., Wright P.E. Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance C-12 heteronuclear Nmr-spectroscopy. J. Am. Chem. Soc. 113:1991;4371-4380.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 4371-4380
    • Palmer, A.G.1    Rance, M.2    Wright, P.E.3
  • 56
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli Ribonuclease Hi - Correlations with structure and function in an active enzyme
    • Mandel A.M., Akke M., Palmer A.G. Backbone dynamics of Escherichia coli Ribonuclease Hi - correlations with structure and function in an active enzyme. J. Mol. Biol. 246:1995;144-163.
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.