메뉴 건너뛰기




Volumn 174, Issue 1, 2005, Pages 43-53

Temperature dependence of protein backbone motion from carbonyl 13C and amide 15N NMR relaxation

Author keywords

Carbonyl relaxation; NMR relaxation; Order parameters; Protein dynamics; Temperature dependence

Indexed keywords

CARBON; COMPUTER SIMULATION; DIFFUSION; NITROGEN; ORGANIC COMPOUNDS; PARAMETER ESTIMATION; PROTEINS; RELAXATION PROCESSES; THERMAL EFFECTS; X RAY ANALYSIS;

EID: 15844366268     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmr.2005.01.008     Document Type: Article
Times cited : (69)

References (45)
  • 2
    • 0031563812 scopus 로고    scopus 로고
    • Contributions to protein entropy and heat capacity from bond vector motions measured by NMR spin relaxation
    • D. Yang, Y.K. Mok, J.D. Forman-Kay, N.A. Farrow, and L.E. Kay Contributions to protein entropy and heat capacity from bond vector motions measured by NMR spin relaxation J. Mol. Biol. 272 1997 790 804
    • (1997) J. Mol. Biol. , vol.272 , pp. 790-804
    • Yang, D.1    Mok, Y.K.2    Forman-Kay, J.D.3    Farrow, N.A.4    Kay, L.E.5
  • 3
    • 0030601792 scopus 로고    scopus 로고
    • Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: Application to protein folding
    • D. Yang, and L.E. Kay Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: Application to protein folding J. Mol. Biol. 263 1996 369 382
    • (1996) J. Mol. Biol. , vol.263 , pp. 369-382
    • Yang, D.1    Kay, L.E.2
  • 4
    • 0035942731 scopus 로고    scopus 로고
    • Microscopic origins of entropy, heat capacity and the glass transition in proteins
    • A.L. Lee, and A.J. Wand Microscopic origins of entropy, heat capacity and the glass transition in proteins Nature 411 2001 501 504
    • (2001) Nature , vol.411 , pp. 501-504
    • Lee, A.L.1    Wand, A.J.2
  • 5
    • 0035940465 scopus 로고    scopus 로고
    • Temperature dependence of dynamics and thermodynamics of the regulatory domain of human cardiac troponin C
    • L. Spyracopoulos, P. Lavigne, M.P. Crump, S.M. Gagne, C.M. Kay, and B.D. Sykes Temperature dependence of dynamics and thermodynamics of the regulatory domain of human cardiac troponin C Biochemistry 40 2001 12541 12551
    • (2001) Biochemistry , vol.40 , pp. 12541-12551
    • Spyracopoulos, L.1    Lavigne, P.2    Crump, M.P.3    Gagne, S.M.4    Kay, C.M.5    Sykes, B.D.6
  • 6
    • 0043194166 scopus 로고    scopus 로고
    • Temperature dependence of domain motions of calmodulin probed by NMR relaxation at multiple fields
    • S.-L. Chang, A. Szabo, and N. Tjandra Temperature dependence of domain motions of calmodulin probed by NMR relaxation at multiple fields J. Am. Chem. Soc. 125 2003 11379 11384
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11379-11384
    • Chang, S.-L.1    Szabo, A.2    Tjandra, N.3
  • 7
    • 0037165750 scopus 로고    scopus 로고
    • General framework for studying the dynamics of folded and nonfolded proteins by NMR relaxation spectroscopy and MD simulation
    • J.J. Prompers, and R. Bruschweiler General framework for studying the dynamics of folded and nonfolded proteins by NMR relaxation spectroscopy and MD simulation J. Am. Chem. Soc. 124 2002 4522 4534
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 4522-4534
    • Prompers, J.J.1    Bruschweiler, R.2
  • 8
    • 0000386638 scopus 로고
    • Proton magnetic relaxation and spin diffusion in proteins
    • A. Kalk, and H.J.C. Berendsen 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
    • 0346969535 scopus 로고    scopus 로고
    • Amide proton relaxation measurements employing a highly deuterated protein
    • T.S. Ulmer, I.D. Campbell, and J. Boyd Amide proton relaxation measurements employing a highly deuterated protein J. Magn. Reson. 166 2004 190 201
    • (2004) J. Magn. Reson. , vol.166 , pp. 190-201
    • Ulmer, T.S.1    Campbell, I.D.2    Boyd, J.3
  • 11
    • 0242299095 scopus 로고    scopus 로고
    • 13C transverse relaxation measurements to sample protein backbone dynamics
    • 13C transverse relaxation measurements to sample protein backbone dynamics Magn. Reson. Chem. 41 2003 853 865
    • (2003) Magn. Reson. Chem. , vol.41 , pp. 853-865
    • Mulder, F.A.A.1    Akke, M.2
  • 12
    • 0029383122 scopus 로고
    • Carbonyl-carbon relaxation rates reveal a dynamic heterogeneity of the polypeptide backbone in villin 14T
    • K.T. Dayie, and G. Wagner Carbonyl-carbon relaxation rates reveal a dynamic heterogeneity of the polypeptide backbone in villin 14T J. Magn. Reson. Series B 109 1995 105 108
    • (1995) J. Magn. Reson. Series B , vol.109 , pp. 105-108
    • Dayie, K.T.1    Wagner, G.2
  • 13
    • 0001920774 scopus 로고    scopus 로고
    • Backbone dynamics of proteins derived from carbonyl carbon relaxation times at 500, 600 and 800 MHz: Application to ribonuclease T1
    • J. Engelke, and H. Ruterjans Backbone dynamics of proteins derived from carbonyl carbon relaxation times at 500, 600 and 800 MHz: Application to ribonuclease T1 J. Biomol. NMR 9 1997 63 78
    • (1997) J. Biomol. NMR , vol.9 , pp. 63-78
    • Engelke, J.1    Ruterjans, H.2
  • 14
    • 0030981715 scopus 로고    scopus 로고
    • 15N-enriched proteins using high-resolution nuclear magnetic resonance
    • 15N-enriched proteins using high-resolution nuclear magnetic resonance J. Am. Chem. Soc. 119 1997 7797 7806
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 7797-7806
    • Dayie, K.T.1    Wagner, G.2
  • 16
    • 0032581920 scopus 로고    scopus 로고
    • Anisotropic intramolecular backbone dynamics of ubiquitin characterized by NMR relaxation and MD computer simulation
    • S.F. Lienin, T. Bremi, B. Brutscher, R. Bruschweiler, and R.R. Ernst Anisotropic intramolecular backbone dynamics of ubiquitin characterized by NMR relaxation and MD computer simulation J. Am. Chem. Soc. 120 1998 9870 9879
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9870-9879
    • Lienin, S.F.1    Bremi, T.2    Brutscher, B.3    Bruschweiler, R.4    Ernst, R.R.5
  • 18
    • 1842503159 scopus 로고    scopus 로고
    • Carbonyl carbon transverse relaxation dispersion measurements and ms-μs timescale motion in a protein hydrogen bond network
    • R. Ishima, J. Baber, J.M. Louis, and D.A. Torchia Carbonyl carbon transverse relaxation dispersion measurements and ms-μs timescale motion in a protein hydrogen bond network J. Biomol. NMR 29 2 2004 187 198
    • (2004) J. Biomol. NMR , vol.29 , Issue.2 , pp. 187-198
    • Ishima, R.1    Baber, J.2    Louis, J.M.3    Torchia, D.A.4
  • 19
    • 0038037171 scopus 로고    scopus 로고
    • Temperature dependence of anisotropic protein backbone dynamics
    • T. Wang, S. Cai, and E.R. Zuiderweg Temperature dependence of anisotropic protein backbone dynamics J. Am. Chem. Soc. 125 28 2003 8639 8643
    • (2003) J. Am. Chem. Soc. , vol.125 , Issue.28 , pp. 8639-8643
    • Wang, T.1    Cai, S.2    Zuiderweg, E.R.3
  • 20
    • 0037176836 scopus 로고    scopus 로고
    • 13CO) NMR relaxation and computational molecular dynamics
    • 13CO) NMR relaxation and computational molecular dynamics Biochemistry 41 2002 2655 2666
    • (2002) Biochemistry , vol.41 , pp. 2655-2666
    • Pang, Y.1    Buck, M.2    Zuiderweg, E.R.3
  • 22
    • 0030752071 scopus 로고    scopus 로고
    • Locally anisotropic internal polypeptide backbone dynamics by NMR relaxation
    • T. Bremi, and R. Bruschweiler Locally anisotropic internal polypeptide backbone dynamics by NMR relaxation J. Am. Chem. Soc. 119 1997 6672 6673
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 6672-6673
    • Bremi, T.1    Bruschweiler, R.2
  • 23
    • 0034738040 scopus 로고    scopus 로고
    • Ubiquitin backbone motion studies via NH-C′Cα dipolar-dipolar and C′-C′Cα/NH CSA-dipolar cross-correlated relaxation
    • T. Carlomagno, M. Maurer, M. Hennig, and C. Griesinger Ubiquitin backbone motion studies via NH-C′Cα dipolar-dipolar and C′- C′Cα/NH CSA-dipolar cross-correlated relaxation J. Am. Chem. Soc. 122 2000 5105 5113
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 5105-5113
    • Carlomagno, T.1    Maurer, M.2    Hennig, M.3    Griesinger, C.4
  • 25
    • 0000041361 scopus 로고
    • A common-sense approach to peak picking in 2-dimensional, 3-dimensional, and 4-dimensional spectra using automatic computer-analysis of contour diagrams
    • D.S. Garrett, R. Powers, A.M. Gronenborn, and G.M. Clore A common-sense approach to peak picking in 2-dimensional, 3-dimensional, and 4-dimensional spectra using automatic computer-analysis of contour diagrams J. Magn. Reson. 95 1991 214 220
    • (1991) J. Magn. Reson. , vol.95 , pp. 214-220
    • Garrett, D.S.1    Powers, R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 26
    • 0024449503 scopus 로고
    • 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease
    • 15N 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
  • 27
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • M. Piotto, V. Saudek, and V. Sklenar Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions J. Biomol. NMR 2 1992 661 665
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 30
    • 0000987483 scopus 로고    scopus 로고
    • An off-resonance rotating frame relaxation experiment for the investigation of macromolecular dynamics using adiabatic rotations
    • F.A.A. Mulder, R.A. de Graff, R. Kaptein, and R. Boelens An off-resonance rotating frame relaxation experiment for the investigation of macromolecular dynamics using adiabatic rotations J. Magn. Reson. 131 1998 351 357
    • (1998) J. Magn. Reson. , vol.131 , pp. 351-357
    • Mulder, F.A.A.1    De Graff, R.A.2    Kaptein, R.3    Boelens, R.4
  • 31
    • 44949273876 scopus 로고
    • Symmetric pulses to induce arbitrary flip angles with compensation for RF inhomogeneity and resonance offsets
    • M. Garwood, and Y. Ke Symmetric pulses to induce arbitrary flip angles with compensation for RF inhomogeneity and resonance offsets J. Magn. Reson. 94 1991 511 525
    • (1991) J. Magn. Reson. , vol.94 , pp. 511-525
    • Garwood, M.1    Ke, Y.2
  • 34
    • 0034684181 scopus 로고    scopus 로고
    • Measurement of proton, nitrogen and carbonyl chemical shielding anisotropies in a protein dissolved in a dilute liquid crystalline phase
    • G. Cornilescu, and A. Bax Measurement of proton, nitrogen and carbonyl chemical shielding anisotropies in a protein dissolved in a dilute liquid crystalline phase J. Am. Chem. Soc. 122 2002 10143 10154
    • (2002) J. Am. Chem. Soc. , vol.122 , pp. 10143-10154
    • Cornilescu, G.1    Bax, A.2
  • 35
    • 0029812794 scopus 로고    scopus 로고
    • 13C J couplings between carbonyl and carbonyl/carboxyl carbons in isotopically enriched proteins
    • 13C J couplings between carbonyl and carbonyl/carboxyl carbons in isotopically enriched proteins J. Am. Chem. Soc. 118 1996 8170 8171
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8170-8171
    • Hu, J.-S.1    Bax, A.2
  • 36
    • 0034679115 scopus 로고    scopus 로고
    • 13CO chemical shift anisotropy tensors in solution
    • 13CO chemical shift anisotropy tensors in solution J. Am. Chem. Soc. 122 2000 4841 4842
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 4841-4842
    • Pang, Y.1    Zuiderweg, E.R.2
  • 37
    • 3142693910 scopus 로고    scopus 로고
    • Determination of chemical shift anisotropy tensors of carbonyl nuclei in proteins through cross-correlated relaxation in NMR
    • F. Cisnetti, K. Loth, P. Pelupessy, and G. Bodenhausen Determination of chemical shift anisotropy tensors of carbonyl nuclei in proteins through cross-correlated relaxation in NMR ChemPhysChem 5 2004 807 814
    • (2004) ChemPhysChem , vol.5 , pp. 807-814
    • Cisnetti, F.1    Loth, K.2    Pelupessy, P.3    Bodenhausen, G.4
  • 39
  • 40
    • 0000387787 scopus 로고
    • 14N electric field gradient tensor orientations with respect to the molecular frame in a polypeptide
    • 14N electric field gradient tensor orientations with respect to the molecular frame in a polypeptide J. Am. Chem. Soc. 114 1992 5312 5321
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 5312-5321
    • Teng, Q.1    Iqbal, M.2    Cross, T.A.3
  • 42
    • 0033106580 scopus 로고    scopus 로고
    • 13C chemical shift tensors and secondary structure of poly-l-alanine by solid-state two-dimensional spin-echo NMR and ab initio chemical shielding calculation
    • 13C chemical shift tensors and secondary structure of poly-l-alanine by solid-state two-dimensional spin-echo NMR and ab initio chemical shielding calculation Magn. Reson. Chem. 37 1999 303 311
    • (1999) Magn. Reson. Chem. , vol.37 , pp. 303-311
    • Asakawa, N.1    Takenoiri, M.2    Sato, D.3    Sakurai, M.4    Inoue, Y.5
  • 44
    • 0033595535 scopus 로고    scopus 로고
    • 15N chemical Shift anisotropy and chemical exchange contributions
    • 15N chemical Shift anisotropy and chemical exchange contributions J. Am. Chem. Soc. 121 1999 8577 8582
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 8577-8582
    • Fushman, D.1    Tjandra, N.2    Cowburn, D.3
  • 45
    • 4544283595 scopus 로고    scopus 로고
    • Site-specific variations of carbonyl chemical shift anisotropies in proteins
    • P.R.L. Markwick, and M. Sattler Site-specific variations of carbonyl chemical shift anisotropies in proteins J. Am. Chem. Soc. 126 2004 11424 11425
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 11424-11425
    • Markwick, P.R.L.1    Sattler, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.