메뉴 건너뛰기




Volumn 47, Issue 2, 2010, Pages 155-162

Comparison of fast backbone dynamics at amide nitrogen and carbonyl sites in dematin headpiece C-terminal domain and its S74E mutant

Author keywords

Backbone dynamics; Carbonyl dynamics; Dematin headpiece; Fast motions; Model free; NMR relaxation

Indexed keywords

AMIDE; CARBON 13; CARBONYL DERIVATIVE; ERYTHROCYTE BAND 4.9 PROTEIN; NITROGEN; NITROGEN 15; PEPTIDE;

EID: 77954690322     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-010-9417-9     Document Type: Article
Times cited : (3)

References (48)
  • 1
    • 0001365263 scopus 로고
    • Influence of crosscorrelation between dipolar and chemical-shift anisotropy relaxation mechanisms upon the transverse relaxation rates of N-15 in macromolecules
    • Boyd J, Hommel U, Krishnan VV (1991) Influence of crosscorrelation between dipolar and chemical-shift anisotropy relaxation mechanisms upon the transverse relaxation rates of N-15 in macromolecules. Chem Phys Lett 187:317-324
    • (1991) Chem Phys Lett , vol.187 , pp. 317-324
    • Boyd, J.1    Hommel, U.2    Krishnan, V.V.3
  • 2
    • 0030752071 scopus 로고    scopus 로고
    • Locally anisotropic internal polypeptide backbone dynamics by NMR relaxation
    • Bremi T, Bruschweiler R (1997) Locally anisotropic internal polypeptide backbone dynamics by NMR relaxation. J Am Chem Soc 119:6672-6673
    • (1997) J Am Chem Soc , vol.119 , pp. 6672-6673
    • Bremi, T.1    Bruschweiler, R.2
  • 3
    • 0034418635 scopus 로고    scopus 로고
    • Principles and applications of cross-correlated relaxation in biomolecules
    • Brutscher B (2000) Principles and applications of cross-correlated relaxation in biomolecules. Concepts Magn Reson 12:207-229
    • (2000) Concepts Magn Reson , vol.12 , pp. 207-229
    • Brutscher, B.1
  • 4
    • 0031992526 scopus 로고    scopus 로고
    • Quantitative investigation of dipole-CSA cross-correlated relaxation by ZQ/DQ spectroscopy
    • Brutscher B, Skrynnikov NR, Bremi T, Bruschweiler R, Ernst RR (1998) Quantitative investigation of dipole-CSA cross-correlated relaxation by ZQ/DQ spectroscopy. J Magn Reson 130:346-351
    • (1998) J Magn Reson , vol.130 , pp. 346-351
    • Brutscher, B.1    Skrynnikov, N.R.2    Bremi, T.3    Bruschweiler, R.4    Ernst, R.R.5
  • 5
    • 15844366268 scopus 로고    scopus 로고
    • Temperature dependence of protein backbone motion from carbonyl C-13 and amide N-15 NMR relaxation
    • Chang SL, Tjandra N (2005) Temperature dependence of protein backbone motion from carbonyl C-13 and amide N-15 NMR relaxation. J Magn Reson 174:43-53
    • (2005) J Magn Reson , vol.174 , pp. 43-53
    • Chang, S.L.1    Tjandra, N.2
  • 6
    • 3142693910 scopus 로고    scopus 로고
    • Determination of chemical shift anisotropy tensors of carbonyl nuclei in proteins through cross-correlated relaxation in NMR
    • Cisnetti F, Loth K, Pelupessy P, Bodenhausen G (2004) Determination of chemical shift anisotropy tensors of carbonyl nuclei in proteins through cross-correlated relaxation in NMR. Chemphyschem 5:807-814
    • (2004) Chemphyschem , vol.5 , pp. 807-814
    • Cisnetti, F.1    Loth, K.2    Pelupessy, P.3    Bodenhausen, G.4
  • 7
    • 0025046144 scopus 로고
    • Deviations from the simple 2-parameter model-free approach to the interpretation of N-15 nuclear magnetic-relaxation of proteins
    • Clore GM, Szabo A, Bax A, Kay LE, Driscoll PC, Gronenborn AM (1990) Deviations from the simple 2-parameter model-free approach to the interpretation of N-15 nuclear magnetic-relaxation of proteins. J Am Chem Soc 112:4989-4991
    • (1990) J Am Chem Soc , vol.112 , pp. 4989-4991
    • Clore, G.M.1    Szabo, A.2    Bax, A.3    Kay, L.E.4    Driscoll, P.C.5    Gronenborn, A.M.6
  • 8
    • 0038068865 scopus 로고    scopus 로고
    • FAST-Modelfree: A program for rapid automated analysis of solution NMR spin-relaxation data
    • Cole R, Loria JP (2003) FAST-Modelfree: a program for rapid automated analysis of solution NMR spin-relaxation data. J Biomol NMR 26:203-213
    • (2003) J Biomol NMR , vol.26 , pp. 203-213
    • Cole, R.1    Loria, J.P.2
  • 11
    • 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
    • Engelke J, Ruterjans H (1997) Backbone dynamics of proteins derived from carbonyl carbon relaxation times at 500, 600 and 800 MHz: application to ribonuclease T1. J Biomol NMR 9:63-78
    • (1997) J Biomol NMR , vol.9 , pp. 63-78
    • Engelke, J.1    Ruterjans, H.2
  • 13
    • 33846626899 scopus 로고    scopus 로고
    • A H-1-NMR thermometer suitable for cryoprobes
    • Findeisen M, Brand T, Berger S (2007) A H-1-NMR thermometer suitable for cryoprobes. Magn Reson Chem 45:175-178
    • (2007) Magn Reson Chem , vol.45 , pp. 175-178
    • Findeisen, M.1    Brand, T.2    Berger, S.3
  • 15
    • 1542349982 scopus 로고    scopus 로고
    • The NMR structure of dematin headpiece reveals a dynamic loop that is conformationally altered upon phosphorylation at a distal site
    • Frank BS, Vardar D, Chishti AH, McKnight CJ (2004) The NMR structure of dematin headpiece reveals a dynamic loop that is conformationally altered upon phosphorylation at a distal site. J Biol Chem 279:7909-7916
    • (2004) J Biol Chem , vol.279 , pp. 7909-7916
    • Frank, B.S.1    Vardar, D.2    Chishti, A.H.3    McKnight, C.J.4
  • 16
    • 34250858152 scopus 로고    scopus 로고
    • Functional dynamics of response regulators using NMR relaxation techniques
    • Gardino AK, Kern D (2007) Functional dynamics of response regulators using NMR relaxation techniques. Methods Enzymol 423:149-156
    • (2007) Methods Enzymol , vol.423 , pp. 149-156
    • Gardino, A.K.1    Kern, D.2
  • 17
    • 48549112585 scopus 로고
    • Interference effects in the relaxation of a pair of unlike spin-1/2 nuclei
    • Goldman M (1984) Interference effects in the relaxation of a pair of unlike spin-1/2 nuclei. J Magn Reson 60:437-452
    • (1984) J Magn Reson , vol.60 , pp. 437-452
    • Goldman, M.1
  • 18
    • 0027966793 scopus 로고
    • Hydrogen-bonding of carboxyl groups in solid-state amino-acids and peptides- comparison of carbon chemical shielding, infrared frequencies, and structures
    • Gu ZT, Zambrano R, McDermott A (1994) Hydrogen-bonding of carboxyl groups in solid-state amino-acids and peptides- comparison of carbon chemical shielding, infrared frequencies, and structures. J Am Chem Soc 116:6368-6372
    • (1994) J Am Chem Soc , vol.116 , pp. 6368-6372
    • Gu, Z.T.1    Zambrano, R.2    McDermott, A.3
  • 19
    • 32044451299 scopus 로고    scopus 로고
    • A phosphorylation-induced conformation change in dematin headpiece
    • Jiang ZG, McKnight CJ (2006) A phosphorylation-induced conformation change in dematin headpiece. Structure 14:379-387
    • (2006) Structure , vol.14 , pp. 379-387
    • Jiang, Z.G.1    McKnight, C.J.2
  • 20
    • 44949291986 scopus 로고
    • 3-dimensional tripleresonance NMR-spectroscopy of isotopically enriched proteins
    • Kay LE, Ikura M, Tschudin R, Bax A (1990) 3-dimensional tripleresonance NMR-spectroscopy of isotopically enriched proteins. J Magn Reson 89:496-514
    • (1990) J Magn Reson , vol.89 , pp. 496-514
    • Kay, L.E.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 21
    • 0032500073 scopus 로고    scopus 로고
    • Alternative splicing and structure of the human erythroid dematin gene
    • Kim AC, Azim AC, Chishti AH (1998) Alternative splicing and structure of the human erythroid dematin gene. Biochim Biophys Acta 1398:382-386
    • (1998) Biochim Biophys Acta , vol.1398 , pp. 382-386
    • Kim, A.C.1    Azim, A.C.2    Chishti, A.H.3
  • 22
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wuthrich K (1996) MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graphics 14:51-55
    • (1996) J Mol Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 23
    • 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
  • 24
    • 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
    • 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
    • (2005) J Am Chem Soc , vol.127 , pp. 6062-6068
    • Loth, K.1    Pelupessy, P.2    Bodenhausen, G.3
  • 25
    • 28044463992 scopus 로고    scopus 로고
    • Correlated dynamics of consecutive residues reveal transient and cooperative unfolding of secondary structure in proteins
    • Lundstrom P, Mulder FAA, Akke M (2005) Correlated dynamics of consecutive residues reveal transient and cooperative unfolding of secondary structure in proteins. Proc Natl Acad Sci USA 102:16984-16989
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16984-16989
    • Lundstrom, P.1    Mulder, F.A.A.2    Akke, M.3
  • 26
    • 0028941877 scopus 로고
    • Backbone dynamics of escherichia-coli ribonuclease Hi-Correlations with Structure and Function in an Active Enzyme
    • Mandel AM, Akke M, Palmer AG (1995) Backbone dynamics of escherichia-coli ribonuclease Hi-Correlations with Structure and Function in an Active Enzyme. J Mol Biol 246:144-163
    • (1995) J Mol Biol , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3
  • 27
    • 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
  • 28
    • 4544283595 scopus 로고    scopus 로고
    • Site-specific variations of carbonyl chemical shift anisotropies in proteins
    • Markwick PRL, Sattler M (2004) Site-specific variations of carbonyl chemical shift anisotropies in proteins. J Am Chem Soc 126: 11424-11425
    • (2004) J Am Chem Soc , vol.126 , pp. 11424-11425
    • Markwick, P.R.L.1    Sattler, M.2
  • 29
    • 33645834303 scopus 로고    scopus 로고
    • Review-New tools provide new insights in NMR studies of protein dynamics
    • Mittermaier A, Kay LE (2006) Review-New tools provide new insights in NMR studies of protein dynamics. Science 312:224-228
    • (2006) Science , vol.312 , pp. 224-228
    • Mittermaier, A.1    Kay, L.E.2
  • 31
    • 0028044572 scopus 로고
    • Backbone dynamics of (1-71) bacterioopsin studied by 2-dimensional H-1-N-15 NMR-spectroscopy
    • Orekhov VY, Pervushin KV, Arseniev AS (1994) Backbone dynamics of (1-71) bacterioopsin studied by 2-dimensional H-1-N-15 NMR-spectroscopy. Eur J Biochem 219:887-896
    • (1994) Eur J Biochem , vol.219 , pp. 887-896
    • Orekhov, V.Y.1    Pervushin, K.V.2    Arseniev, A.S.3
  • 32
    • 4243155782 scopus 로고    scopus 로고
    • NMR characterization of the dynamics of biomacromolecules
    • Palmer AG (2004) NMR characterization of the dynamics of biomacromolecules. Chem Rev 104:3623-3640
    • (2004) Chem Rev , vol.104 , pp. 3623-3640
    • Palmer, A.G.1
  • 33
    • 0037176836 scopus 로고    scopus 로고
    • Backbone dynamics of the ribonuclease binase active site area using multinuclear (N-15 and (CO)-C-13) NMR relaxation and computational molecular dynamics
    • Pang Y, Buck M, Zuiderweg ERP (2002) Backbone dynamics of the ribonuclease binase active site area using multinuclear (N-15 and (CO)-C-13) 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
  • 34
    • 0037510001 scopus 로고    scopus 로고
    • Correlated motions of successive amide N-H bonds in proteins
    • Pelupessy P, Ravindranathan S, Bodenhausen G (2003) Correlated motions of successive amide N-H bonds in proteins. J Biomol NMR 25:265-280
    • (2003) J Biomol NMR , vol.25 , pp. 265-280
    • Pelupessy, P.1    Ravindranathan, S.2    Bodenhausen, G.3
  • 35
    • 34047246826 scopus 로고    scopus 로고
    • Accurate measurement of longitudinal cross-relaxation rates in nuclear magnetic resonance
    • Pelupessy P, Ferrage F, Bodenhausen G (2007) Accurate measurement of longitudinal cross-relaxation rates in nuclear magnetic resonance. J Chem Phys 126:134508
    • (2007) J Chem Phys , vol.126 , pp. 134508
    • Pelupessy, P.1    Ferrage, F.2    Bodenhausen, G.3
  • 36
    • 0000660936 scopus 로고
    • Mapping of spectral density-functions using heteronuclear NMR relaxation measurements
    • Peng JW, Wagner G (1992) Mapping of spectral density-functions using heteronuclear NMR relaxation measurements. J Magn Reson 98:308-332
    • (1992) J Magn Reson , vol.98 , pp. 308-332
    • Peng, J.W.1    Wagner, G.2
  • 38
    • 0042367594 scopus 로고    scopus 로고
    • Evaluation of backbone proton positions and dynamics in a small protein by liquid crystal NMR spectroscopy
    • Ulmer TS, Ramirez BE, Delaglio F, Bax A (2003) Evaluation of backbone proton positions and dynamics in a small protein by liquid crystal NMR spectroscopy. J Am Chem Soc 125:9179-9191
    • (2003) J Am Chem Soc , vol.125 , pp. 9179-9191
    • Ulmer, T.S.1    Ramirez, B.E.2    Delaglio, F.3    Bax, A.4
  • 39
    • 57549109368 scopus 로고    scopus 로고
    • Slow motions in chicken villin headpiece subdomain probed by cross-correlated NMR relaxation of amide NH bonds in successive residues
    • Vugmeyster L, McKnight CJ (2008) Slow motions in chicken villin headpiece subdomain probed by cross-correlated NMR relaxation of amide NH bonds in successive residues. Biophys J 95:5941-5950
    • (2008) Biophys J , vol.95 , pp. 5941-5950
    • Vugmeyster, L.1    McKnight, C.J.2
  • 40
    • 57549099407 scopus 로고    scopus 로고
    • Phosphorylation-induced changes in backbone dynamics of the dematin headpiece Cterminal domain
    • Vugmeyster L, McKnight CJ (2009) Phosphorylation-induced changes in backbone dynamics of the dematin headpiece Cterminal domain. J Biomol NMR 43:39-50
    • (2009) J Biomol NMR , vol.43 , pp. 39-50
    • Vugmeyster, L.1    McKnight, C.J.2
  • 41
    • 0037668073 scopus 로고    scopus 로고
    • Beyond the decoupling approximation in the model free approach for the interpretation of NMR relaxation of macromolecules in solution
    • Vugmeyster L, Raleigh DP, Palmer AG, Vugmeister BE (2003) Beyond the decoupling approximation in the model free approach for the interpretation of NMR relaxation of macromolecules in solution. J Am Chem Soc 125:8400-8404
    • (2003) J Am Chem Soc , vol.125 , pp. 8400-8404
    • Vugmeyster, L.1    Raleigh, D.P.2    Palmer, A.G.3    Vugmeister, B.E.4
  • 42
    • 2442500664 scopus 로고    scopus 로고
    • Cross-correlated relaxation in NMR of macromolecules in the presence of fast and slow internal dynamics
    • Vugmeyster L, Pelupessy P, Vugmeister BE, Abergel D, Bodenhausen G (2004) Cross-correlated relaxation in NMR of macromolecules in the presence of fast and slow internal dynamics. C R Phys 5:377-386
    • (2004) C R Phys , vol.5 , pp. 377-386
    • Vugmeyster, L.1    Pelupessy, P.2    Vugmeister, B.E.3    Abergel, D.4    Bodenhausen, G.5
  • 43
    • 0038037171 scopus 로고    scopus 로고
    • Temperature dependence of anisotropic protein backbone dynamics
    • Wang TZ, Cai S, Zuiderweg ERP (2003) Temperature dependence of anisotropic protein backbone dynamics. J Am Chem Soc 125: 8639-8643
    • (2003) J Am Chem Soc , vol.125 , pp. 8639-8643
    • Wang, T.Z.1    Cai, S.2    Zuiderweg, E.R.P.3
  • 44
    • 12444278203 scopus 로고    scopus 로고
    • Changes in calmodulin main-chain dynamics upon ligand binding revealed by cross-correlated NMR relaxation measurements
    • Wang TZ, Frederick KK, Igumenova TI, Wand AJ, Zuiderweg ERP (2005) Changes in calmodulin main-chain dynamics upon ligand binding revealed by cross-correlated NMR relaxation measurements. J Am Chem Soc 127:828-829
    • (2005) J Am Chem Soc , vol.127 , pp. 828-829
    • Wang, T.Z.1    Frederick, K.K.2    Igumenova, T.I.3    Wand, A.J.4    Zuiderweg, E.R.P.5
  • 45
    • 33749188590 scopus 로고    scopus 로고
    • Quantifying Lipari-Szabo modelfree parameters from 13CO NMR relaxation experiments
    • Wang T, Weaver DS, Cai S, Zuiderweg ERP (2006) Quantifying Lipari-Szabo modelfree parameters from 13CO NMR relaxation experiments. J Biomol NMR 36:79-102
    • (2006) J Biomol NMR , vol.36 , pp. 79-102
    • Wang, T.1    Weaver, D.S.2    Cai, S.3    Zuiderweg, E.R.P.4
  • 46
    • 0034832980 scopus 로고    scopus 로고
    • Solid-state C-13 NMR chemical shift anisotropy tensors of polypeptides
    • Wei YF, Lee DK, Ramamoorthy A (2001) Solid-state C-13 NMR chemical shift anisotropy tensors of polypeptides. J Am Chem Soc 123:6118-6126
    • (2001) J Am Chem Soc , vol.123 , pp. 6118-6126
    • Wei, Y.F.1    Lee, D.K.2    Ramamoorthy, A.3
  • 47
    • 0032513009 scopus 로고    scopus 로고
    • A study of protein side-chain dynamics from new H-2 auto-correlation and C-13 cross-correlation NMR experiments: application to the Nterminal SH3 domain from drk
    • Yang DW, Mittermaier A, Mok YK, Kay LE (1998) A study of protein side-chain dynamics from new H-2 auto-correlation and C-13 cross-correlation NMR experiments: application to the Nterminal SH3 domain from drk. J Mol Biol 276:939-954
    • (1998) J Mol Biol , vol.276 , pp. 939-954
    • Yang, D.W.1    Mittermaier, A.2    Mok, Y.K.3    Kay, L.E.4
  • 48
    • 33645233083 scopus 로고    scopus 로고
    • Flexibility and plasticity of human centrin 2 binding to the xeroderma pigmentosum group c protein (XPC) from nuclear excision repair
    • Yang A, Miron S, Mouawad L, Duchambon P, Bloquit Y, Craescu CT (2006) Flexibility and plasticity of human centrin 2 binding to the xeroderma pigmentosum group c protein (XPC) from nuclear excision repair. Biochemistry 45:3653-3663
    • (2006) Biochemistry , vol.45 , pp. 3653-3663
    • Yang, A.1    Miron, S.2    Mouawad, L.3    Duchambon, P.4    Bloquit, Y.5    Craescu, C.T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.