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Volumn 146, Issue 1, 2000, Pages 188-195

Peptide Internal Motions on Nanosecond Time Scale Derived from Direct Fitting of 13C and 15N NMR Spectral Density Functions

Author keywords

13C and 15N relaxation; Internal motions; NMR; Peptide; Spectral densities

Indexed keywords

CARBON; NITROGEN; PEPTIDE;

EID: 0034264355     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmre.2000.2148     Document Type: Article
Times cited : (18)

References (35)
  • 2
    • 0028674384 scopus 로고
    • Investigation of protein motions via relaxation measurements
    • J. W. Peng and G. Wagner, Investigation of protein motions via relaxation measurements, Methods Enzymol. 239, 563-596 (1994).
    • (1994) Methods Enzymol. , vol.239 , pp. 563-596
    • Peng, J.W.1    Wagner, G.2
  • 3
    • 13844324197 scopus 로고
    • Characterization of biomolecular structure and dynamics by NMR cross relaxation
    • R. Brueschweiler and D. A. Case, Characterization of biomolecular structure and dynamics by NMR cross relaxation, Prog. NMR Spectrosc. 26, 27-58 (1994).
    • (1994) Prog. NMR Spectrosc. , vol.26 , pp. 27-58
    • Brueschweiler, R.1    Case, D.A.2
  • 4
    • 0030338305 scopus 로고    scopus 로고
    • Theory and practice of nuclear spin relaxation in proteins
    • K. T. Dayie and G. Wagner, Theory and practice of nuclear spin relaxation in proteins, Ann. Rev. Phys. Chem. 47, 243-282 (1996).
    • (1996) Ann. Rev. Phys. Chem. , vol.47 , pp. 243-282
    • Dayie, K.T.1    Wagner, G.2
  • 6
    • 0002978605 scopus 로고
    • A general formalism for the analysis of NMR relaxation measurements on systems with multiple degrees of freedom
    • R. King and O. Jardetzky, A general formalism for the analysis of NMR relaxation measurements on systems with multiple degrees of freedom, Chem. Phys. Lett. 55, 15-18 (1978).
    • (1978) Chem. Phys. Lett. , vol.55 , pp. 15-18
    • King, R.1    Jardetzky, O.2
  • 7
    • 33845553743 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. II. Analysis of experimental results
    • G. Lipari and A. Szabo, Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. II. Analysis of experimental results, J. Am. Chem. Soc. 104, 4559-4570 (1982).
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 10
    • 0023339183 scopus 로고
    • Enhanced resolution of fluorescence anisotropy decays by simultaneous analysis of progressively quenched samples. Applications to anisotropic rotations and to protein dynamics
    • J. R. Lakowicz, H. Cherek, I. Gryczynski, N. Joshi, and M. L. Johnson, Enhanced resolution of fluorescence anisotropy decays by simultaneous analysis of progressively quenched samples. Applications to anisotropic rotations and to protein dynamics, Biophys. J. 51, 755-768 (1987).
    • (1987) Biophys. J. , vol.51 , pp. 755-768
    • Lakowicz, J.R.1    Cherek, H.2    Gryczynski, I.3    Joshi, N.4    Johnson, M.L.5
  • 11
    • 0030034685 scopus 로고    scopus 로고
    • Dynamics of the three methionyl side-chains of Streptomyces subtilisin inhibitor. Deuterium NMR studies in solution and in the solid state
    • A. Tamura, M. Matsushita, A. Naito, S. Kojima, K. I. Miura, and K. Akasaka, Dynamics of the three methionyl side-chains of Streptomyces subtilisin inhibitor. Deuterium NMR studies in solution and in the solid state, Protein Sci. 5, 127-139 (1996).
    • (1996) Protein Sci. , vol.5 , pp. 127-139
    • Tamura, A.1    Matsushita, M.2    Naito, A.3    Kojima, S.4    Miura, K.I.5    Akasaka, K.6
  • 12
    • 0026784152 scopus 로고
    • Mapping of the spectral densities of N-H bond motions in eglin c using heteronuclear relaxation experiments
    • J. W. Peng and G. Wagner, Mapping of the spectral densities of N-H bond motions in eglin c using heteronuclear relaxation experiments, Biochemistry 31, 8571-8586 (1992).
    • (1992) Biochemistry , vol.31 , pp. 8571-8586
    • Peng, J.W.1    Wagner, G.2
  • 13
    • 0029009067 scopus 로고
    • The hydrophobic-staple motif and a role for loop-residues in α-helix stability and protein folding
    • V. Munoz, F. J. Blanco, and L. Serrano, The hydrophobic-staple motif and a role for loop-residues in α-helix stability and protein folding, Struct. Biol. 2, 380-385 (1995).
    • (1995) Struct. Biol. , vol.2 , pp. 380-385
    • Munoz, V.1    Blanco, F.J.2    Serrano, L.3
  • 15
    • 13444269041 scopus 로고
    • Computer-optimized decoupling scheme for wideband applications and low-level operation
    • A. J. Shaka, P. B. Barker, and R. Freeman, Computer-optimized decoupling scheme for wideband applications and low-level operation, J. Magn. Reson. 64, 547-552 (1985).
    • (1985) J. Magn. Reson. , vol.64 , pp. 547-552
    • Shaka, A.J.1    Barker, P.B.2    Freeman, R.3
  • 19
    • 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
    • A. G. Palmer III, N. J. Skelton, W. J. Chasin, P. E Wright, and M. Rance, 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, 699-711 (1992).
    • (1992) Mol. Phys. , vol.75 , pp. 699-711
    • Palmer A.G. III1    Skelton, N.J.2    Chasin, W.J.3    Wright, P.E.4    Rance, M.5
  • 20
    • 12044251259 scopus 로고
    • Solvent suppression with simetrically shifted pulses
    • S. H. Smallcombe, Solvent suppression with simetrically shifted pulses, J. Am. Chem. Soc. 115, 4769-4785 (1993).
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 4769-4785
    • Smallcombe, S.H.1
  • 23
    • 0033577288 scopus 로고    scopus 로고
    • Sensitivity improvement of transverse relaxation-optimized spectroscopy
    • J. Loria, M. Rance, and A. Palmer III, Sensitivity improvement of transverse relaxation-optimized spectroscopy, J. Am. Chem. Soc. 121, 2331-2332 (1999).
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2331-2332
    • Loria, J.1    Rance, M.2    Palmer A. III3
  • 24
    • 48749147783 scopus 로고
    • An improved sequence for broadband decoupling: WALTZ-16
    • A. J. Shaka, J. Keeler, T. Frenkiel, and R. Freeman, An improved sequence for broadband decoupling: WALTZ-16, J. Magn. Reson. 52, 335-338 (1983).
    • (1983) J. Magn. Reson. , vol.52 , pp. 335-338
    • Shaka, A.J.1    Keeler, J.2    Frenkiel, T.3    Freeman, R.4
  • 25
    • 36849099862 scopus 로고
    • Spin-lattice relaxation measurements in slowly relaxing complex spectra
    • J. L. Markley, W. J. Horsley, and M. P. Klein, Spin-lattice relaxation measurements in slowly relaxing complex spectra, J. Chem. Phys. 55, 3604-3605 (1971).
    • (1971) J. Chem. Phys. , vol.55 , pp. 3604-3605
    • Markley, J.L.1    Horsley, W.J.2    Klein, M.P.3
  • 26
    • 0027787894 scopus 로고
    • 2O in protein NMR. Application to sensitivity enhancement and NOE measurements
    • 2O in protein NMR. Application to sensitivity enhancement and NOE measurements, J. Am. Chem. Soc. 115, 12,593-12,594 (1993).
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 12593-12594
    • Grzesiek, S.1    Bax, A.2
  • 27
    • 0000308780 scopus 로고    scopus 로고
    • Using the model free approach to analyze NMR relaxation data in cases of anisotropic molecular diffusion
    • V. A. Daragan and K. M. Mayo, Using the model free approach to analyze NMR relaxation data in cases of anisotropic molecular diffusion, J. Phys. Chem. 103, 6829-6843 (1999).
    • (1999) J. Phys. Chem. , vol.103 , pp. 6829-6843
    • Daragan, V.A.1    Mayo, K.M.2
  • 28
    • 36149012348 scopus 로고
    • Asymmetric diffusion tensor for molecular rotations
    • L. D. Favro, Asymmetric diffusion tensor for molecular rotations, Phys. Rev. 119, 53-59 (1960).
    • (1960) Phys. Rev. , vol.119 , pp. 53-59
    • Favro, L.D.1
  • 29
    • 33644625296 scopus 로고
    • Nuclear spin relaxation in ellipsoids undergoing rotational Brownian motion
    • D. E. Woessner, Nuclear spin relaxation in ellipsoids undergoing rotational Brownian motion, J. Chem. Phys. 37, 647-653 (1962).
    • (1962) J. Chem. Phys. , vol.37 , pp. 647-653
    • Woessner, D.E.1
  • 30
    • 36849114522 scopus 로고
    • Effect of anisotropic molecular rotational diffusion on nuclear magnetic relaxation in liquids
    • W. T. Huntress, Jr., Effect of anisotropic molecular rotational diffusion on nuclear magnetic relaxation in liquids, J. Chem. Phys. 48, 3524-3534 (1967).
    • (1967) J. Chem. Phys. , vol.48 , pp. 3524-3534
    • Huntress W.T., Jr.1
  • 31
    • 0029973119 scopus 로고    scopus 로고
    • Direct observation of fast protein folding: The initial collapse of apomyoglobin
    • R. M. Ballew, J. Sabelko, and M. Gruebele, Direct observation of fast protein folding: The initial collapse of apomyoglobin, Proc. Natl. Acad. Sci. USA 93, 5759-5764 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5759-5764
    • Ballew, R.M.1    Sabelko, J.2    Gruebele, M.3
  • 32
    • 0038502170 scopus 로고    scopus 로고
    • Folding dynamics and mechanism of β-hairpin formation
    • V. Munoz, P. A. Thompson, J. Hofrichter, and W. A. Eaton, Folding dynamics and mechanism of β-hairpin formation, Nature 380, 196-199 (1997).
    • (1997) Nature , vol.380 , pp. 196-199
    • Munoz, V.1    Thompson, P.A.2    Hofrichter, J.3    Eaton, W.A.4
  • 34
    • 0031049285 scopus 로고    scopus 로고
    • Backbone and side-chain dynamics of residues in a partially folded β-sheet peptide from platelet factor-4
    • V. Daragan, E. E. Ilyina, C. G. Fields, G. B. Fields, and K. H. Mayo, Backbone and side-chain dynamics of residues in a partially folded β-sheet peptide from platelet factor-4, Protein Sci. 6, 355-363 (1997).
    • (1997) Protein Sci. , vol.6 , pp. 355-363
    • Daragan, V.1    Ilyina, E.E.2    Fields, C.G.3    Fields, G.B.4    Mayo, K.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.