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Volumn 24, Issue 1, 2005, Pages 1-9

The concept of effective correlation times for describing backbone motions in proteins. Part I. A residue-per-residue self-consistent analysis of multifield 15N relaxation parameters

Author keywords

15N relaxation; Chemical shift anisotropy; Exchange contributions; NMR spectroscopy; Proteins

Indexed keywords

NITROGEN 15; PROTEIN; PROTON;

EID: 18444404914     PISSN: 15466086     EISSN: 15525023     Source Type: Journal    
DOI: 10.1002/cmr.a.20026     Document Type: Article
Times cited : (3)

References (21)
  • 1
    • 0028674384 scopus 로고
    • Investigations of protein motions via relaxation measurements
    • Peng JW, Wagner G. 1994. Investigations of protein motions via relaxation measurements. Methods Enzymol 239:563-596.
    • (1994) Methods Enzymol , vol.239 , pp. 563-596
    • Peng, J.W.1    Wagner, G.2
  • 2
    • 0030217514 scopus 로고    scopus 로고
    • Nuclear magnetic resonance studies of biopolymer dynamics
    • Palmer AG III, Williams J, McDermott A. 1996. Nuclear magnetic resonance studies of biopolymer dynamics. J Phys Chem 100:13293-13310.
    • (1996) J Phys Chem , vol.100 , pp. 13293-13310
    • Palmer III, A.G.1    Williams, J.2    McDermott, A.3
  • 3
    • 0034746293 scopus 로고    scopus 로고
    • 15N-NMR relaxation as a probe for helical intrinsic propensity: The case of the unfolded D2 domain of annexin I
    • Ochsenbein F, Guerois R, Neumann J-M, Sanson A, Guittet E, van Heijenoort C. 2001. 15N-NMR relaxation as a probe for helical intrinsic propensity: the case of the unfolded D2 domain of annexin I. J Biomol NMR 19:3-18.
    • (2001) J Biomol NMR , vol.19 , pp. 3-18
    • Ochsenbein, F.1    Guerois, R.2    Neumann, J.-M.3    Sanson, A.4    Guittet, E.5    Van Heijenoort, C.6
  • 4
    • 0034823221 scopus 로고    scopus 로고
    • Simulated and NMR derived backbone dynamics of a protein with significant flexibility: A comparison of spectral densities for the βARK PH domain
    • Pfeiffer S, Fushman D, Cowburn D. 2001. Simulated and NMR derived backbone dynamics of a protein with significant flexibility: A comparison of spectral densities for the βARK PH domain. J Am Chem Soc 123: 3021-3036.
    • (2001) J Am Chem Soc , vol.123 , pp. 3021-3036
    • Pfeiffer, S.1    Fushman, D.2    Cowburn, D.3
  • 6
    • 0038062647 scopus 로고    scopus 로고
    • 15NH backbone dynamics of protein GB1: Comparison of order parameters and correlation times derived using various "model free" approaches
    • 15NH backbone dynamics of protein GB1: Comparison of order parameters and correlation times derived using various "model free" approaches. J Phys Chem B 107: 2602-2609.
    • (2003) J Phys Chem B , vol.107 , pp. 2602-2609
    • Idiyatullin, D.1    Daragan, V.A.2    Mayo, K.H.3
  • 7
    • 0037176836 scopus 로고    scopus 로고
    • 13CO) NMR relaxation and computational molecular dynamics
    • 13CO) NMR relaxation and computational molecular dynamics. Biochemistry 41:2655-2666.
    • (2002) Biochemistry , vol.41 , pp. 2655-2666
    • Pang, Y.1    Buck, M.2    Zuiderweg, E.R.P.3
  • 10
    • 0029029566 scopus 로고
    • Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling
    • Brüschweiler R, Liao X, Wright PE. 1995. Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling. Science 268:886-889.
    • (1995) Science , vol.268 , pp. 886-889
    • Brüschweiler, R.1    Liao, X.2    Wright, P.E.3
  • 11
    • 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. 1982. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J Am Chem Soc 104:4546-4559.
    • (1982) J Am Chem Soc , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 13
    • 0032511359 scopus 로고    scopus 로고
    • 15N chemical shift anisotropy relaxation interference: Unambiguous determination of rotational diffusion tensors and chemical exchange effects in biological macromolecules
    • 15N chemical shift anisotropy relaxation interference: Unambiguous determination of rotational diffusion tensors and chemical exchange effects in biological macromolecules. J Am Chem Soc 120:7905-7915.
    • (1998) J Am Chem Soc , vol.120 , pp. 7905-7915
    • Kroenke, C.D.1    Loria, J.P.2    Lee, L.K.3    Rance, M.4    Palmer III, A.G.5
  • 15
    • 18444375358 scopus 로고    scopus 로고
    • On the calculation of cross-correlation spectral density functions within the model-free approach
    • Canet D, Bouguet-Bonnet S, Mutzenhardt P. 2003. On the calculation of cross-correlation spectral density functions within the model-free approach. Concepts Magn Reson A 19:65-70.
    • (2003) Concepts Magn Reson A , vol.19 , pp. 65-70
    • Canet, D.1    Bouguet-Bonnet, S.2    Mutzenhardt, P.3
  • 16
    • 0001125152 scopus 로고
    • 15N chemical shift interaction tensors in a peptide bond by three-dimensional solid-state NMR spectroscopy
    • 15N chemical shift interaction tensors in a peptide bond by three-dimensional solid-state NMR spectroscopy. J Am Chem Soc 117:6148-6149.
    • (1995) J Am Chem Soc , vol.117 , pp. 6148-6149
    • Wu, C.H.1    Ramamoorthy, A.2    Gierasch, L.M.3    Opella, S.J.4
  • 17
    • 0023261246 scopus 로고
    • Determination of the nitrogen-15 and carbon-13 chemical shift tensors of L-[13C]alanyl-L-[15N]alanine from the dipole-coupled powder patterns
    • Hartzell CJ, Whitfield M, Oas TG, Drobny GP. 1987. Determination of the nitrogen-15 and carbon-13 chemical shift tensors of L-[13C]alanyl-L-[15N]alanine from the dipole-coupled powder patterns. J Am Chem Soc 109:5966-5969.
    • (1987) J Am Chem Soc , vol.109 , pp. 5966-5969
    • Hartzell, C.J.1    Whitfield, M.2    Oas, T.G.3    Drobny, G.P.4
  • 18
    • 0023261245 scopus 로고
    • The amide nitrogen-15 chemical shift tensors of four peptides determined from carbon-13 dipole-coupled chemical shift powder patterns
    • Oas TG, Hartzell CJ, Dahlquist FW, Drobny GP. 1987. The amide nitrogen-15 chemical shift tensors of four peptides determined from carbon-13 dipole-coupled chemical shift powder patterns. J Am Chem Soc 109: 5962-5966.
    • (1987) J Am Chem Soc , vol.109 , pp. 5962-5966
    • Oas, T.G.1    Hartzell, C.J.2    Dahlquist, F.W.3    Drobny, G.P.4
  • 19
    • 58149364138 scopus 로고
    • 15N nuclear magnetic relaxation data of proteins
    • 15N nuclear magnetic relaxation data of proteins. J Magn Reson B 109:100-104.
    • (1995) J Magn Reson B , vol.109 , pp. 100-104
    • Habazettl, J.1    Wagner, G.2
  • 20
    • 0034728579 scopus 로고    scopus 로고
    • The static magnetic field dependence of chemical exchange linebroadening defines the NMR chemical shift time scale
    • Millet O, Loria JP, Kroenke CD, Pons M, Palmer AG III. 2000. The static magnetic field dependence of chemical exchange linebroadening defines the NMR chemical shift time scale. J Am Chem Soc 122:2867-2877.
    • (2000) J Am Chem Soc , vol.122 , pp. 2867-2877
    • Millet, O.1    Loria, J.P.2    Kroenke, C.D.3    Pons, M.4    Palmer III, A.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.