메뉴 건너뛰기




Volumn 38, Issue 3, 2007, Pages 255-266

Vibrational averaging of chemical shift anisotropies in model peptides

Author keywords

Chemical shift; Peptide; Vibrations

Indexed keywords

ACETAMIDE DERIVATIVE; CARBON; N METHYLACETAMIDE; N-METHYLACETAMIDE; NITROGEN; PEPTIDE; PHENYLALANINE; UNCLASSIFIED DRUG;

EID: 34748866639     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-007-9164-8     Document Type: Article
Times cited : (34)

References (34)
  • 2
    • 0000797345 scopus 로고
    • On the simulation of quantum systems: Path integral methods
    • Berne BJ, Thirumalai D (1986) On the simulation of quantum systems: path integral methods. Annu Rev Phys Chem 37:401-424
    • (1986) Annu Rev Phys Chem , vol.37 , pp. 401-424
    • Berne, B.J.1    Thirumalai, D.2
  • 3
    • 0026734453 scopus 로고
    • Normal modes and NMR order parameters in proteins
    • Brüschweiler R (1992) Normal modes and NMR order parameters in proteins. J Am Chem Soc 114:5341-5344
    • (1992) J Am Chem Soc , vol.114 , pp. 5341-5344
    • Brüschweiler, R.1
  • 4
    • 33645786604 scopus 로고    scopus 로고
    • Importance of the cmap correction to the charmm22 protein force field: Dynamics of hen lysozyme
    • Buck M, BouguetBonnet S, Pastor RW, MacKerell AD (2006) Importance of the CMAP Correction to the CHARMM22 Protein Force Field: dynamics of Hen Lysozyme. Biophys J 90:L36-L38
    • (2006) Biophys J , vol.90
    • Buck, M.1    BouguetBonnet, S.2    Pastor, R.W.3    MacKerell, A.D.4
  • 5
    • 0032705883 scopus 로고    scopus 로고
    • Internal and overall peptide group motion in proteins: Molecular dynamics simulations for Lysozyme compared with results from X-ray and NMR spectroscopy
    • Buck M, Karplus M (1999) Internal and overall peptide group motion in proteins: molecular dynamics simulations for Lysozyme compared with results from X-ray and NMR spectroscopy. J Am Chem Soc 121:9645-9658
    • (1999) J Am Chem Soc , vol.121 , pp. 9645-9658
    • Buck, M.1    Karplus, M.2
  • 6
    • 33846846421 scopus 로고    scopus 로고
    • 13C' CSA tensor principal components for ubiquitin: Correlation between tensor components and hydrogen bonding
    • DOI 10.1021/ja066835c
    • Burton RA, Tjandra N (2007) Residue-specific 13C' CSA tensor principal components for Ubiquitin: correlation between tensor components and hydrogen bonding. J Am Chem Soc 129:1321-1326 (Pubitemid 46208604)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.5 , pp. 1321-1326
    • Burton, R.A.1    Tjandra, N.2
  • 7
    • 0032719896 scopus 로고    scopus 로고
    • Calculations of NMR dipolar coupling strengths in model peptides
    • Case DA (1999) Calculations of NMR dipolar coupling strengths in model peptides. J Biomol NMR 15:95-102
    • (1999) J Biomol NMR , vol.15 , pp. 95-102
    • Case, D.A.1
  • 10
    • 13644264053 scopus 로고    scopus 로고
    • 15N CSA magnitudes and orientations in ubiquitin are revealed by joint analysis of longitudinal and transverse NMR relaxation
    • DOI 10.1021/ja045956e
    • Damberg P, Jarvet J, Graslund A (2005) Limited variations in 15N CSA magnitudes and orientations in Ubiquitin are revealed by joint analysis of longitudinal and transverse NMR relaxation. J Am Chem Soc 127:1995-2005 (Pubitemid 40229183)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.6 , pp. 1995-2005
    • Damberg, P.1    Jarvet, J.2    Graslund, A.3
  • 12
    • 0032558085 scopus 로고    scopus 로고
    • 15N chemical shift anisotropy from NMR relaxation data. Ubiquitin as a test example [5]
    • DOI 10.1021/ja980565j
    • 15N chemical shift anisotropy from NMR relaxation data. Ubiquitin as a test example. J Am Chem Soc 120:7109-7110 (Pubitemid 28378372)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.28 , pp. 7109-7110
    • Fushman, D.1    Cowburn, D.2
  • 14
    • 0141502348 scopus 로고    scopus 로고
    • Characterization of the overall and local dynamics of a protein with intermediate rotational anisotropy: Differentiating between conformational exchange and anisotropic diffusion in the B3 domain of protein G
    • DOI 10.1023/A:1025467918856
    • Hall JB, Fushman D (2003) Characterization of the overall and local dynamics of a protein with intermediate rotational anisotropy: differentiating between conformational exchange and anisotropic diffusion in the B3 domain of protein G. J Biomol NMR 27:261-275 (Pubitemid 37185125)
    • (2003) Journal of Biomolecular NMR , vol.27 , Issue.3 , pp. 261-275
    • Hall, J.B.1    Fushman, D.2
  • 15
    • 33745362452 scopus 로고    scopus 로고
    • 15N relaxation measurements at several fields. Implications for backbone order parameters
    • DOI 10.1021/ja060406x
    • 15N relaxation measurements at several fields. Implications for backbone order parameters. J Am Chem Soc 128:7855-7870 (Pubitemid 43945727)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.24 , pp. 7855-7870
    • Hall, J.B.1    Fushman, D.2
  • 16
    • 0000279972 scopus 로고
    • Influence of vibrational motion on solid state line shapes and NMR relaxation
    • Henry ER, Szabo A (1985) Influence of vibrational motion on solid state line shapes and NMR relaxation. J Chem Phys 82:4753-4761
    • (1985) J Chem Phys , vol.82 , pp. 4753-4761
    • Henry, E.R.1    Szabo, A.2
  • 18
    • 0031208109 scopus 로고    scopus 로고
    • Theory and simulation of vibrational effects on structural measurements by solid-state nuclear magnetic resonance
    • Ishii Y, Terao T, Hayashi S (1997) Theory and simulation of vibrational effects on structural measurements by solid-state nuclear magnetic resonance. J Chem Phys 107:2760-2774 (Pubitemid 127568893)
    • (1997) Journal of Chemical Physics , vol.107 , Issue.8 , pp. 2760-2774
    • Ishii, Y.1    Terao, T.2    Hayashi, S.3
  • 21
    • 0033520723 scopus 로고    scopus 로고
    • 15N chemical shift anisotropy in Escherichia coli ribonuclease H in solution
    • 15N chemical shift anisotropy in Escherichia coli ribonuclease H in solution. J Am Chem Soc 121:10119-10125
    • (1999) J Am Chem Soc , vol.121 , pp. 10119-10125
    • Kroenke, C.D.1    Rance, M.2    Palmer III, A.G.3
  • 22
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. I. Theory and range of validity
    • Lipari G, Szabo A (1982) Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. I. 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
  • 23
    • 17744366182 scopus 로고    scopus 로고
    • Chemical shift anisotropy tensors of carbonyl, nitrogen, and amide proton nuclei in proteins through cross-correlated relaxation in NMR spectroscopy
    • DOI 10.1021/ja042863o
    • Loth K, Pelupessy P, Bodenhausen G (2005) Chemical shift anisotropy tensors of carbonyl, nitrogen, and amide proton nuclei in proteins through cross-correlated relaxation in NMR spectroscopy. J Am Chem Soc 127:6062-6068 (Pubitemid 40577663)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.16 , pp. 6062-6068
    • Loth, K.1    Pelupessy, P.2    Bodenhausen, G.3
  • 24
    • 0038061657 scopus 로고    scopus 로고
    • Analysis of the pyramidalization of the peptide group nitrogen: Implications for molecular mechanics energy functions
    • Mannfors BE, Mirkin NG, Palmo K, Krimm S (2003) Analysis of the pyramidalization of the peptide group nitrogen: implications for molecular mechanics energy functions. J Phys Chem A 107:1825-1832
    • (2003) J Phys Chem A , vol.107 , pp. 1825-1832
    • Mannfors, B.E.1    Mirkin, N.G.2    Palmo, K.3    Krimm, S.4
  • 25
    • 4544283595 scopus 로고    scopus 로고
    • Site-specific variations of carbonyl chemical shift anisotropies in proteins
    • DOI 10.1021/ja047859r
    • Markwick P R L, Sattler M (2004) Site-specific variations of carbonyl chemical shift anisotropies in proteins. J Am Chem Soc 126:11424-11425 (Pubitemid 39244943)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.37 , pp. 11424-11425
    • Markwick, P.R.L.1    Sattler, M.2
  • 26
    • 33646230997 scopus 로고    scopus 로고
    • A comparison of quantum chemical models for calculating NMR shielding parameters in peptides: Mixed basis set and ONIOM methods combined with a complete basis set extrapolation
    • Moon S, Case DA (2006) A comparison of quantum chemical models for calculating NMR shielding parameters in peptides: mixed basis set and ONIOM methods combined with a complete basis set extrapolation. J Comput Chem 27:825-836
    • (2006) J Comput Chem , vol.27 , pp. 825-836
    • Moon, S.1    Case, D.A.2
  • 28
    • 0032477283 scopus 로고    scopus 로고
    • Determination of relative N-H(N), N-C', C(α)-C', and C(α)-H(α) effective bond lengths in a protein by NMR in a dilute liquid crystalline phase
    • DOI 10.1021/ja9826791
    • Ottiger M, Bax A (1998) Determination of relative N-HN, N-C', and C alpha-H alpha effective bond lengths in a protein by NMR in a dilute liquid crystalline phase. J Am Chem Soc 120:12334-12341 (Pubitemid 28558193)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.47 , pp. 12334-12341
    • Ottiger, M.1    Bax, A.2
  • 30
  • 31
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
    • DOI 10.1126/science.278.5340.1111
    • Tjandra N, Bax A (1997) Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science 278:1111-1114 (Pubitemid 27517889)
    • (1997) Science , vol.278 , Issue.5340 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 32
    • 49049140501 scopus 로고
    • Spin-lattice relaxation in solids
    • Torchia DA, Szabo A (1982) Spin-lattice relaxation in solids. J Magn Reson 49:107-121
    • (1982) J Magn Reson , vol.49 , pp. 107-121
    • Torchia, D.A.1    Szabo, A.2
  • 33
    • 0034102297 scopus 로고    scopus 로고
    • Assessment of zinc finger orientations by residual dipolar coupling constants
    • DOI 10.1023/A:1008302430561
    • Tsui V, Zhu L, Huang TH, Wright PE, Case DA (2000) Assessment of zinc finger orientations by residual dipolar coupling constants. J Biomol NMR 16:9-21 (Pubitemid 30114720)
    • (2000) Journal of Biomolecular NMR , vol.16 , Issue.1 , pp. 9-21
    • Tsui, V.1    Zhu, L.2    Huang, T.-H.3    Wright, P.E.4    Case, D.A.5
  • 34
    • 33846287932 scopus 로고    scopus 로고
    • Effects of zero-point and thermal vibrational averaging on computed NMR properties of a model compound for purine nucleosides
    • Woodford JN, Harbison GS (2006) Effects of zero-point and thermal vibrational averaging on computed NMR properties of a model compound for purine nucleosides. J Chem Theory Comput 2:1464-1475
    • (2006) J Chem Theory Comput , vol.2 , pp. 1464-1475
    • Woodford, J.N.1    Harbison, G.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.