메뉴 건너뛰기




Volumn 45, Issue 4, 2009, Pages 361-372

Simple tests for the validation of multiple field spin relaxation data

Author keywords

Consistency test; Model free analysis; Protein dynamics; Relax program; Spin relaxation

Indexed keywords

BETA LACTAMASE; RETINOL BINDING PROTEIN;

EID: 71049167170     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-009-9381-4     Document Type: Article
Times cited : (18)

References (37)
  • 2
    • 0025046144 scopus 로고
    • Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins
    • DOI 10.1021/ja00168a070
    • GM Clore A Szabo A Bax LE Kay PC Driscoll AM Gronenborn 1990 Deviations from the simple 2-parameter model-free approach to the interpretation of Nitrogen-15 nuclear magnetic-relaxation of proteins J Am Chem Soc 112 4989 4991 10.1021/ja00168a070 (Pubitemid 20285925)
    • (1990) Journal of the American Chemical Society , vol.112 , Issue.12 , 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
  • 4
    • 0037266991 scopus 로고    scopus 로고
    • The use of model selection in the model-free analysis of protein dynamics
    • DOI 10.1023/A:1021902006114
    • EJ d'Auvergne PR Gooley 2003 The use of model selection in the model-free analysis of protein dynamics J Biomol NMR 25 25 39 10.1023/A:1021902006114 (Pubitemid 36181759)
    • (2003) Journal of Biomolecular NMR , vol.25 , Issue.1 , pp. 25-39
    • D'Auvergne, E.J.1    Gooley, P.R.2
  • 5
    • 38349077155 scopus 로고    scopus 로고
    • Optimisation of NMR dynamic models i. minimisation algorithms and their performance within the model-free and brownian rotational diffusion spaces
    • 10.1007/s10858-007-9214-2
    • EJ d'Auvergne PR Gooley 2008 Optimisation of NMR dynamic models i. minimisation algorithms and their performance within the model-free and brownian rotational diffusion spaces J Biomol NMR 40 107 119 10.1007/s10858-007-9214-2
    • (2008) J Biomol NMR , vol.40 , pp. 107-119
    • D'Auvergne, E.J.1    Gooley, P.R.2
  • 6
    • 38349050193 scopus 로고    scopus 로고
    • Optimisation of NMR dynamic models ii. a new methodology for the dual optimisation of the model-free parameters and the brownian rotational diffusion tensor
    • 10.1007/s10858-007-9213-3
    • EJ d'Auvergne PR Gooley 2008 Optimisation of NMR dynamic models ii. a new methodology for the dual optimisation of the model-free parameters and the brownian rotational diffusion tensor J Biomol NMR 40 121 133 10.1007/s10858-007-9213-3
    • (2008) J Biomol NMR , vol.40 , pp. 121-133
    • D'Auvergne, E.J.1    Gooley, P.R.2
  • 7
    • 23044501324 scopus 로고    scopus 로고
    • PhosphoThr peptide binding globally rigidifies much of the FHA domain from Arabidopsis receptor kinase-associated protein phosphatase
    • DOI 10.1021/bi050414a
    • Z Ding G in Lee X Liang F Gallazzi A Arunima SRV Doren 2005 PhosphoThr peptide binding globally rigidifies much of the FHA domain from Arabidopsis receptor kinase-associated protein phosphatase Biochemistry 44 10119 10134 10.1021/bi050414a (Pubitemid 41076807)
    • (2005) Biochemistry , vol.44 , Issue.30 , pp. 10119-10134
    • Ding, Z.1    Lee, G.-I.2    Liang, X.3    Gallazzi, F.4    Arunima, A.5    Van Doren, S.R.6
  • 8
    • 84976651235 scopus 로고
    • Über die von der molekularkinetischen theorie der wärme geforderte bewegung von in ruhenden flüssigkeiten suspendierten teilchen
    • 10.1002/andp.19053221004
    • A Einstein 1905 Über die von der molekularkinetischen theorie der wärme geforderte bewegung von in ruhenden flüssigkeiten suspendierten teilchen Ann Phys 17 891 921 10.1002/andp.19053221004
    • (1905) Ann Phys , vol.17 , pp. 891-921
    • Einstein, A.1
  • 10
    • 0000285293 scopus 로고    scopus 로고
    • Protein NMR relaxation: Theory, application and outlook
    • 10.1016/S0079-6565(98)00023-5
    • M Fischer A Majumdar ERP Zuiderweg 1998 Protein NMR relaxation: theory, application and outlook Prog Nucl Magn Reson Spectrosc 33 207 272 10.1016/S0079-6565(98)00023-5
    • (1998) Prog Nucl Magn Reson Spectrosc , vol.33 , pp. 207-272
    • Fischer, M.1    Majumdar, A.2    Zuiderweg, E.R.P.3
  • 14
    • 43049128515 scopus 로고    scopus 로고
    • Structure and dynamics of de novo proteins from a designed superfamily of 4-helix bundles
    • DOI 10.1110/ps.073377908
    • A Go S Kim J Baum MH Hecht 2008 Structure and dynamics of de novo proteins from a designed superfamily of 4-helix bundles Protein Sci 17 5 821 832 10.1110/ps.073377908 (Pubitemid 351629577)
    • (2008) Protein Science , vol.17 , Issue.5 , pp. 821-832
    • Go, A.1    Kim, S.2    Baum, J.3    Hecht, M.H.4
  • 15
    • 35048898436 scopus 로고    scopus 로고
    • 15 N transverse relaxation: An NMR spectroscopy application to the study of a folding intermediate with pervasive chemical exchange
    • DOI 10.1021/ja072717t
    • 15 N transverse relaxation: an NMR spectroscopy application to the study of a folding intermediate with pervasive chemical exchange J Am Chem Soc 129 11468 11479 10.1021/ja072717t (Pubitemid 47555566)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.37 , pp. 11468-11479
    • Hansen, D.F.1    Yang, D.2    Feng, H.3    Zhou, Z.4    Wiesner, S.5    Bai, Y.6    Kay, L.E.7
  • 16
    • 70349119250 scopus 로고
    • Regression and time series model selection in small samples
    • 0669.62085 10.1093/biomet/76.2.297 1016020
    • C Hurvich CL Tsai 1989 Regression and time series model selection in small samples Biometrika 76 297 307 0669.62085 10.1093/biomet/76.2.297 1016020
    • (1989) Biometrika , vol.76 , pp. 297-307
    • Hurvich, C.1    Tsai, C.L.2
  • 17
    • 0024449503 scopus 로고
    • 15 N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease
    • 10.1021/bi00449a003
    • 15 N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease Biochemistry 28 8972 8979 10.1021/bi00449a003
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 18
  • 21
    • 0033029875 scopus 로고    scopus 로고
    • Assessing potential bias in the determination of rotational correlation times of proteins by NMR relaxation
    • DOI 10.1023/A:1008304220445
    • AL Lee AJ Wand 1999 Assessing potential bias in the determination of rotational correlation times of proteins by NMR relaxation J Biomol NMR 13 101 112 10.1023/A:1008304220445 (Pubitemid 29089220)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.2 , pp. 101-112
    • Lee, A.L.1    Wand, A.J.2
  • 22
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • 10.1021/ja00381a009
    • G Lipari A Szabo 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 10.1021/ja00381a009
    • (1982) J Am Chem Soc , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 23
    • 33845553743 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results
    • 10.1021/ja00381a010
    • G Lipari A Szabo 1982 Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results J Am Chem Soc 104 4559 4570 10.1021/ja00381a010
    • (1982) J Am Chem Soc , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 24
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme
    • 10.1006/jmbi.1994.0073
    • AM Mandel M Akke AG Palmer 1995 Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme J Mol Biol 246 144 163 10.1006/jmbi.1994.0073
    • (1995) J Mol Biol , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3
  • 25
    • 68949086333 scopus 로고    scopus 로고
    • NMR dynamics of PSE-4 β-lactamase: An interplay of ps-ns order and μs-ms motions in the active site
    • 10.1016/j.bpj.2009.02.068
    • S Morin SM Gagné 2009 NMR dynamics of PSE-4 β-lactamase: an interplay of ps-ns order and μs-ms motions in the active site Biophys J 96 4681 4691 10.1016/j.bpj.2009.02.068
    • (2009) Biophys J , vol.96 , pp. 4681-4691
    • Morin, S.1    Gagné, S.M.2
  • 27
    • 33749007969 scopus 로고    scopus 로고
    • Backbone dynamics of TEM-1 determined by NMR: Evidence for a highly ordered protein
    • DOI 10.1021/bi060414q
    • PY Savard SM Gagné 2006 Backbone dynamics of TEM-1 determined by NMR: evidence for a highly ordered protein Biochemistry 45 11414 11424 10.1021/bi060414q (Pubitemid 44453989)
    • (2006) Biochemistry , vol.45 , Issue.38 , pp. 11414-11424
    • Savard, P.-Y.1    Gagne, S.M.2
  • 28
    • 0028541223 scopus 로고
    • A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization
    • 10.1006/jmrb.1994.1127
    • JM Schurr HP Babcock BS Fujimoto 1994 A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization J Magn Reson Ser B 105 211 224 10.1006/jmrb.1994.1127
    • (1994) J Magn Reson ser B , vol.105 , pp. 211-224
    • Schurr, J.M.1    Babcock, H.P.2    Fujimoto, B.S.3
  • 30
    • 84978694892 scopus 로고
    • Zur kinetischen theorie der brownschen molekularbewegung und der suspensionen
    • 10.1002/andp.19063261405
    • M Smoluchowski 1906 Zur kinetischen theorie der brownschen molekularbewegung und der suspensionen Ann Phys 21 756 780 10.1002/andp. 19063261405
    • (1906) Ann Phys , vol.21 , pp. 756-780
    • Smoluchowski, M.1
  • 31
    • 37349039360 scopus 로고    scopus 로고
    • Functional implications for a prototypical K-turn binding protein from structural and dynamical studies of 15.5K
    • DOI 10.1021/bi701254q
    • SE Soss PF Flynn 2007 Functional implications for a prototypical k-turn binding protein from structural and dynamical studies of 15.5 K Biochemistry 46 14979 14986 10.1021/bi701254q (Pubitemid 350308889)
    • (2007) Biochemistry , vol.46 , Issue.51 , pp. 14979-14986
    • Soss, S.E.1    Flynn, P.F.2
  • 32
    • 0029900275 scopus 로고    scopus 로고
    • 15 N chemical shift anisotropy from quantitative measurement of relaxation interference effects
    • DOI 10.1021/ja960510m
    • 15 N chemical shift anisotropy from quantitative measurement of relaxation interference effects J Am Chem Soc 118 6986 6991 10.1021/ja960510m (Pubitemid 26252043)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.29 , pp. 6986-6991
    • Tjandra, N.1    Szabo, A.2    Bax, A.3
  • 33
    • 0030253418 scopus 로고    scopus 로고
    • 15 N NMR relaxation measurements at two magnetic fields
    • 10.1007/BF00410326
    • 15 N NMR relaxation measurements at two magnetic fields J Biomol NMR 8 273 284 10.1007/BF00410326
    • (1996) J Biomol NMR , vol.8 , pp. 273-284
    • Tjandra, N.1    Wingfield, P.2    Stahl, S.3    Bax, A.4
  • 35
    • 7544221415 scopus 로고    scopus 로고
    • 15 N relaxation experiment
    • 10.1016/j.jmr.2004.06.021 2004JMagR.171.25Y
    • 15 N relaxation experiment J Magn Reson 171 25 36 10.1016/j.jmr.2004.06.021 2004JMagR.171...25Y
    • (2004) J Magn Reson , vol.171 , pp. 25-36
    • Yip, G.N.B.1    Zuiderweg, E.R.P.2
  • 36
    • 25144515100 scopus 로고    scopus 로고
    • Improvement of duty-cycle heating compensation in NMR spin relaxation experiments
    • DOI 10.1016/j.jmr.2005.06.003, PII S109078070500193X
    • GNB Yip ERP Zuiderweg 2005 Improvement of duty-cycle heating compensation in NMR spin relaxation experiments J Magn Reson 176 171 178 10.1016/j.jmr.2005.06.003 2005JMagR.176..171Y (Pubitemid 41336684)
    • (2005) Journal of Magnetic Resonance , vol.176 , Issue.2 , pp. 171-178
    • Yip, G.N.B.1    Zuiderweg, E.R.P.2
  • 37
    • 4444248119 scopus 로고    scopus 로고
    • Gated electron transfers and electron pathways in azurin: A NMR dynamic study at multiple fields and temperatures
    • DOI 10.1016/j.jmb.2004.08.001, PII S0022283604009556
    • AV Zhuravleva DM Korzhnev E Kupce AS Arseniev M Billeter VY Orekhov 2004 Gated electron transfers and electron pathways in azurin: a NMR dynamic study at multiple fields and temperatures J Mol Biol 342 1599 1611 10.1016/j.jmb.2004. 08.001 (Pubitemid 39208681)
    • (2004) Journal of Molecular Biology , vol.342 , Issue.5 , pp. 1599-1611
    • Zhuravleva, A.V.1    Korzhnev, D.M.2    Kupce, E.3    Arseniev, A.S.4    Billeter, M.5    Orekhov, V.Yu.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.