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Volumn 55, Issue 3, 2013, Pages 249-256

Fast hydrogen exchange affects 15N relaxation measurements in intrinsically disordered proteins

Author keywords

15N R 2 relaxation; Hydrogen exchange; Intrinsically disordered protein

Indexed keywords

ALPHA SYNUCLEIN; HYDROGEN;

EID: 84877924088     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-013-9706-1     Document Type: Article
Times cited : (16)

References (40)
  • 1
    • 0037161143 scopus 로고    scopus 로고
    • 15N NMR mobility study on the dicalcium P43 M calbindin D9 k and its mono-La3 + -substituted form
    • 10.1021/bi015945n
    • 15N NMR mobility study on the dicalcium P43 M calbindin D9 k and its mono-La3 + -substituted form. Biochemistry 41:5104-5111
    • (2002) Biochemistry , vol.41 , pp. 5104-5111
    • Bertini, I.1    Carrano, C.J.2    Luchinat, C.3    Piccioli, M.4    Poggi, L.5
  • 2
    • 34548189188 scopus 로고    scopus 로고
    • Structural characterization of the intrinsically unfolded protein beta-synuclein, a natural negative regulator of alpha-synuclein aggregation
    • 10.1016/j.jmb.2007.07.009
    • Bertoncini CW, Rasia RM, Lamberto GR, Binolfi A, Zweckstetter M, Griesinger C, Fernandez CO (2007) Structural characterization of the intrinsically unfolded protein beta-synuclein, a natural negative regulator of alpha-synuclein aggregation. J Mol Biol 372:708-722
    • (2007) J Mol Biol , vol.372 , pp. 708-722
    • Bertoncini, C.W.1    Rasia, R.M.2    Lamberto, G.R.3    Bnfi, A.4    Zweckstetter, M.5    Griesinger, C.6    Fernandez, C.O.7
  • 3
    • 0033595571 scopus 로고    scopus 로고
    • Dynamics of unfolded proteins: Incorporation of distributions of correlation times in the model free analysis of NMR relaxation data
    • 10.1021/ja9910412
    • Buevich AV, Baum J (1999) Dynamics of unfolded proteins: incorporation of distributions of correlation times in the model free analysis of NMR relaxation data. J Am Chem Soc 121:8671-8672
    • (1999) J Am Chem Soc , vol.121 , pp. 8671-8672
    • Buevich, A.V.1    Baum, J.2
  • 4
    • 0034885557 scopus 로고    scopus 로고
    • Backbone dynamics of the natively unfolded pro-peptide of subtilisin by heteronuclear NMR relaxation studies
    • 10.1023/A:1011243116136
    • Buevich AV, Shinde UP, Inouye M, Baum J (2001) Backbone dynamics of the natively unfolded pro-peptide of subtilisin by heteronuclear NMR relaxation studies. J Biomol NMR 20:233-249
    • (2001) J Biomol NMR , vol.20 , pp. 233-249
    • Buevich, A.V.1    Shinde, U.P.2    Inouye, M.3    Baum, J.4
  • 5
    • 0035824545 scopus 로고    scopus 로고
    • Residual structure and dynamics in Parkinson's disease-associated mutants of alpha-synuclein
    • 10.1074/jbc.M106777200
    • Bussell R Jr, Eliezer D (2001) Residual structure and dynamics in Parkinson's disease-associated mutants of alpha-synuclein. J Biol Chem 276:45996-46003
    • (2001) J Biol Chem , vol.276 , pp. 45996-46003
    • Bussell, Jr.R.1    Eliezer, D.2
  • 6
    • 80055065601 scopus 로고    scopus 로고
    • 15N spin relaxation rates
    • 2011JMagR.213.151C 10.1016/j.jmr.2011.09.042
    • 15N spin relaxation rates. J Magn Reson 213:151-157
    • (2011) J Magn Reson , vol.213 , pp. 151-157
    • Chen, J.1    Tjandra, N.2
  • 7
    • 77951667170 scopus 로고    scopus 로고
    • H/D-SOLEXSY experiment for accurate measurement of amide solvent exchange rates: Application to denatured drkN SH3
    • 10.1007/s10858-010-9398-8
    • H/D-SOLEXSY experiment for accurate measurement of amide solvent exchange rates: application to denatured drkN SH3. J Biomol NMR 46:227-244
    • (2010) J Biomol NMR , vol.46 , pp. 227-244
    • Chevelkov, V.1    Xue, Y.2    Rao, D.K.3    Forman-Kay, J.D.4    Skrynnikov, N.R.5
  • 8
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • 10.1146/annurev.biochem.75.101304.123901
    • Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75:333-366
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 9
    • 48249099670 scopus 로고    scopus 로고
    • Hydrogen exchange of monomeric alpha-synuclein shows unfolded structure persists at physiological temperature and is independent of molecular crowding in Escherichia coli
    • 10.1110/ps.033803.107
    • Croke RL, Sallum CO, Watson E, Watt ED, Alexandrescu AT (2008) Hydrogen exchange of monomeric alpha-synuclein shows unfolded structure persists at physiological temperature and is independent of molecular crowding in Escherichia coli. Protein Sci 17:1434-1445
    • (2008) Protein Sci , vol.17 , pp. 1434-1445
    • Croke, R.L.1    Sallum, C.O.2    Watson, E.3    Watt, E.D.4    Alexandrescu, A.T.5
  • 10
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • 10.1007/BF00197809
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277-293
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 11
    • 0035928606 scopus 로고    scopus 로고
    • Hydrogen exchange in peptides and proteins using NMR spectroscopy
    • 10.1016/S0079-6565(01)00032-2
    • Dempsey CE (2001) Hydrogen exchange in peptides and proteins using NMR spectroscopy. Prog Nucl Magn Reson Spectrosc 39:135-170
    • (2001) Prog Nucl Magn Reson Spectrosc , vol.39 , pp. 135-170
    • Dempsey, C.E.1
  • 12
    • 60349087841 scopus 로고    scopus 로고
    • Biophysical characterization of intrinsically disordered proteins
    • 10.1016/j.sbi.2008.12.004
    • Eliezer D (2009) Biophysical characterization of intrinsically disordered proteins. Curr Opin Struct Biol 19:23-30
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 23-30
    • Eliezer, D.1
  • 13
    • 0035815115 scopus 로고    scopus 로고
    • Conformational properties of alpha-synuclein in its free and lipid-associated states
    • 10.1006/jmbi.2001.4538
    • Eliezer D, Kutluay E, Bussell R Jr, Browne G (2001) Conformational properties of alpha-synuclein in its free and lipid-associated states. J Mol Biol 307:1061-1073
    • (2001) J Mol Biol , vol.307 , pp. 1061-1073
    • Eliezer, D.1    Kutluay, E.2    Bussell, Jr.R.3    Browne, G.4
  • 15
    • 0000950943 scopus 로고
    • Measurement of fast proton exchange rates in isotopically labeled compounds
    • 10.1021/ja00077a080
    • Gemmecker G, Jahnke W, Kessler H (1993) Measurement of fast proton exchange rates in isotopically labeled compounds. J Am Chem Soc 115:11620-11621
    • (1993) J Am Chem Soc , vol.115 , pp. 11620-11621
    • Gemmecker, G.1    Jahnke, W.2    Kessler, H.3
  • 16
    • 0035409575 scopus 로고    scopus 로고
    • Alpha-synuclein and neurodegenerative diseases
    • 10.1038/35081564
    • Goedert M (2001) Alpha-synuclein and neurodegenerative diseases. Nat Rev Neurosci 2:492-501
    • (2001) Nat Rev Neurosci , vol.2 , pp. 492-501
    • Goedert, M.1
  • 17
    • 0000955573 scopus 로고
    • Cross relaxation in time-dependent nuclear spin systems: Invariant trajectory approach
    • 1988CPL.152.239G 10.1016/0009-2614(88)87361-5
    • Griesinger C, Ernst RR (1988) Cross relaxation in time-dependent nuclear spin systems: invariant trajectory approach. Chem Phys Lett 152:239-247
    • (1988) Chem Phys Lett , vol.152 , pp. 239-247
    • Griesinger, C.1    Ernst, R.R.2
  • 18
    • 0042531551 scopus 로고    scopus 로고
    • Implications of using approximate Bloch-McConnell equations in NMR analyses of chemically exchanging systems: Application to the electron self-exchange of plastocyanin
    • 2003JMagR.163.215F 10.1016/S1090-7807(03)00062-4
    • Hansen DF, Led JJ (2003) Implications of using approximate Bloch-McConnell equations in NMR analyses of chemically exchanging systems: application to the electron self-exchange of plastocyanin. J Magn Reson 163:215-227
    • (2003) J Magn Reson , vol.163 , pp. 215-227
    • Hansen, D.F.1    Led, J.J.2
  • 19
    • 0031989849 scopus 로고    scopus 로고
    • Accurate quantitation of water-amide proton exchange rates using the phase-modulated CLEAN chemical EXchange (CLEANEX-PM) approach with a Fast-HSQC (FHSQC) detection scheme
    • 10.1023/A:1008276004875
    • Hwang TL, van Zijl PC, Mori S (1998) Accurate quantitation of water-amide proton exchange rates using the phase-modulated CLEAN chemical EXchange (CLEANEX-PM) approach with a Fast-HSQC (FHSQC) detection scheme. J Biomol NMR 11:221-226
    • (1998) J Biomol NMR , vol.11 , pp. 221-226
    • Hwang, T.L.1    Van Zijl, P.C.2    Mori, S.3
  • 21
    • 33846031611 scopus 로고    scopus 로고
    • Measuring fast hydrogen exchange rates by NMR spectroscopy
    • 2007JMagR.184.108K 10.1016/j.jmr.2006.09.022
    • Kateb F, Pelupessy P, Bodenhausen G (2007) Measuring fast hydrogen exchange rates by NMR spectroscopy. J Magn Reson 184:108-113
    • (2007) J Magn Reson , vol.184 , pp. 108-113
    • Kateb, F.1    Pelupessy, P.2    Bodenhausen, G.3
  • 22
    • 0024449503 scopus 로고
    • 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease
    • 10.1021/bi00449a003
    • 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry 28:8972-8979
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 23
    • 0037063506 scopus 로고    scopus 로고
    • An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates
    • 10.1021/ja0204776
    • Korzhnev DM, Skrynnikov NR, Millet O, Torchia DA, Kay LE (2002) An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates. J Am Chem Soc 124:10743-10753
    • (2002) J Am Chem Soc , vol.124 , pp. 10743-10753
    • Korzhnev, D.M.1    Skrynnikov, N.R.2    Millet, O.3    Torchia, D.A.4    Kay, L.E.5
  • 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
    • Mandel AM, Akke M, Palmer AG 3rd (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 Iii., A.G.3
  • 25
    • 0010957050 scopus 로고
    • Reaction rates by nuclear magnetic resonance
    • 1958JChPh.28.430M 10.1063/1.1744152
    • McConnell HM (1958) Reaction rates by nuclear magnetic resonance. J Chem Phys 28:430-431
    • (1958) J Chem Phys , vol.28 , pp. 430-431
    • McConnell, H.M.1
  • 26
    • 33644538922 scopus 로고    scopus 로고
    • Temperature-induced reversible conformational change in the first 100 residues of alpha-synuclein
    • 10.1110/ps.051867106
    • McNulty BC, Tripathy A, Young GB, Charlton LM, Orans J, Pielak GJ (2006) Temperature-induced reversible conformational change in the first 100 residues of alpha-synuclein. Protein Sci 15:602-608
    • (2006) Protein Sci , vol.15 , pp. 602-608
    • McNulty, B.C.1    Tripathy, A.2    Young, G.B.3    Charlton, L.M.4    Orans, J.5    Pielak, G.J.6
  • 27
    • 33846913510 scopus 로고    scopus 로고
    • Atomic-level characterization of disordered protein ensembles
    • 10.1016/j.sbi.2007.01.009
    • Mittag T, Forman-Kay JD (2007) Atomic-level characterization of disordered protein ensembles. Curr Opin Struct Biol 17:3-14
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 3-14
    • Mittag, T.1    Forman-Kay, J.D.2
  • 28
    • 70449769332 scopus 로고    scopus 로고
    • Observing biological dynamics at atomic resolution using NMR
    • 10.1016/j.tibs.2009.07.004
    • Mittermaier AK, Kay LK (2009) Observing biological dynamics at atomic resolution using NMR. Trends Biochem Sci 34:601-611
    • (2009) Trends Biochem Sci , vol.34 , pp. 601-611
    • Mittermaier, A.K.1    Kay, L.K.2
  • 29
    • 4243155782 scopus 로고    scopus 로고
    • NMR characterization of the dynamics of biomacromolecules
    • 10.1021/cr030413t
    • Palmer AG III (2004) NMR characterization of the dynamics of biomacromolecules. Chem Rev 104:3623-3640
    • (2004) Chem Rev , vol.104 , pp. 3623-3640
    • Palmer Iii., A.G.1
  • 30
    • 0000486802 scopus 로고
    • Suppression of the effects of cross-correlation between dipolar and anisotropic chemical shift relaxation mechanisms in the measurement of spin-spin relaxation rates
    • 1992MolPh.75.699P 10.1080/00268979200100511
    • Palmer AG III, Skelton NJ, Chazin WJ, Wright PE, Rance M (1992) Suppression of the effects of cross-correlation between dipolar and anisotropic chemical shift relaxation mechanisms in the measurement of spin-spin relaxation rates. Mol Phys 75:699-711
    • (1992) Mol Phys , vol.75 , pp. 699-711
    • Palmer Iii., A.G.1    Skelton, N.J.2    Chazin, W.J.3    Wright, P.E.4    Rance, M.5
  • 31
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond-to- millisecond motions in biological macromolecules
    • 10.1016/S0076-6879(01)39315-1
    • Palmer AG III, Kroenke CD, Loria JP (2001) Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Method Enzymol 339:204-238
    • (2001) Method Enzymol , vol.339 , pp. 204-238
    • Palmer Iii., A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 32
    • 0033090632 scopus 로고    scopus 로고
    • Detection of intermolecular chemical exchange through decorrelation of two-spin order
    • 1999JMagR.137.276S 10.1006/jmre.1998.1666
    • Skrynnikov NR, Ernst RR (1999) Detection of intermolecular chemical exchange through decorrelation of two-spin order. J Magn Reson 137:276-280
    • (1999) J Magn Reson , vol.137 , pp. 276-280
    • Skrynnikov, N.R.1    Ernst, R.R.2
  • 33
    • 0037432547 scopus 로고    scopus 로고
    • Quantitative NMR studies of high molecular weight proteins: Application to domain orientation and ligand binding in the 723 residue enzyme malate synthase G
    • 10.1016/S0022-2836(03)00238-9
    • Tugarinov V, Kay LE (2003) Quantitative NMR studies of high molecular weight proteins: application to domain orientation and ligand binding in the 723 residue enzyme malate synthase G. J Mol Biol 327:1121-1133
    • (2003) J Mol Biol , vol.327 , pp. 1121-1133
    • Tugarinov, V.1    Kay, L.E.2
  • 34
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • 10.1002/1097-0134(20001115)41:3<415: AID-PROT130>3.0.CO;2-7
    • Uversky VN, Gillespie JR, Fink AL (2000) Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins 41:415-427
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 36
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • 10.1021/bi961799n
    • Weinreb PH, Zhen W, Poon AW, Conway KA, Lansbury PT Jr (1996) NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 35:13709-13715
    • (1996) Biochemistry , vol.35 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3    Conway, K.A.4    Lansbury, Jr.P.T.5
  • 37
    • 60349101875 scopus 로고    scopus 로고
    • Linking folding and binding
    • 10.1016/j.sbi.2008.12.003
    • Wright PE, Dyson HJ (2009) Linking folding and binding. Curr Opin Struct Biol 19:31-38
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 31-38
    • Wright, P.E.1    Dyson, H.J.2
  • 38
    • 42649142233 scopus 로고    scopus 로고
    • Characterization of conformational and dynamic properties of natively unfolded human and mouse alpha-synuclein ensembles by NMR: Implication for aggregation
    • 10.1016/j.jmb.2008.03.017
    • Wu K-P, Kim S, Fela DA, Baum J (2008) Characterization of conformational and dynamic properties of natively unfolded human and mouse alpha-synuclein ensembles by NMR: implication for aggregation. J Mol Biol 378:1104-1115
    • (2008) J Mol Biol , vol.378 , pp. 1104-1115
    • Wu, K.-P.1    Kim, S.2    Fela, D.A.3    Baum, J.4
  • 39
    • 68149132468 scopus 로고    scopus 로고
    • Structural reorganization of alpha-synuclein at low pH observed by NMR and REMD simulations
    • 10.1016/j.jmb.2009.06.063
    • Wu K-P, Weinstock DS, Narayanan C, Levy RM, Baum J (2009) Structural reorganization of alpha-synuclein at low pH observed by NMR and REMD simulations. J Mol Biol 391:784-796
    • (2009) J Mol Biol , vol.391 , pp. 784-796
    • Wu, K.-P.1    Weinstock, D.S.2    Narayanan, C.3    Levy, R.M.4    Baum, J.5
  • 40
    • 0028966761 scopus 로고
    • Rapid amide proton exchange rates in peptides and proteins measured by solvent quenching and two-dimensional NMR
    • 10.1002/pro.5560040420
    • Zhang YZ, Paterson Y, Roder H (1995) Rapid amide proton exchange rates in peptides and proteins measured by solvent quenching and two-dimensional NMR. Protein Sci 4:804-814
    • (1995) Protein Sci , vol.4 , pp. 804-814
    • Zhang, Y.Z.1    Paterson, Y.2    Roder, H.3


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