메뉴 건너뛰기




Volumn 45, Issue 4, 2009, Pages 343-349

Comprehensive determination of 3JHNHα for unfolded proteins using 13C′-resolved spin-echo difference spectroscopy

Author keywords

Conformation; HNHA; IDP; IUP; J coupling

Indexed keywords

CARBON 13; NEUROLIGIN; NEUROLIGIN 3; NITROGEN; PROTON; UNCLASSIFIED DRUG;

EID: 71049194723     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-009-9382-3     Document Type: Article
Times cited : (9)

References (29)
  • 1
    • 66849106554 scopus 로고    scopus 로고
    • An expanding arsenal of experimental methods yields an explosion of insights into protein folding mechanisms
    • 10.1038/nsmb.1592
    • AI Bartlett SE Radford 2009 An expanding arsenal of experimental methods yields an explosion of insights into protein folding mechanisms Nature Struct Mol Biol 16 6 582 588 10.1038/nsmb.1592
    • (2009) Nature Struct Mol Biol , vol.16 , Issue.6 , pp. 582-588
    • Bartlett, A.I.1    Radford, S.E.2
  • 2
    • 0026861304 scopus 로고
    • Precise vicinal coupling constants 3JHN-alpha in proteins from nonlinear fits of J-modulated [N-15, H-1]-COSY experiments
    • 10.1007/BF01875320
    • M Billeter D Neri G Otting YQ Qian K Wuthrich 1992 Precise vicinal coupling constants 3JHN-alpha in proteins from nonlinear fits of J-modulated [N-15, H-1]-COSY experiments J Biomol NMR 2 3 257 274 10.1007/BF01875320
    • (1992) J Biomol NMR , vol.2 , Issue.3 , pp. 257-274
    • Billeter, M.1    Neri, D.2    Otting, G.3    Qian, Y.Q.4    Wuthrich, K.5
  • 3
    • 0034715485 scopus 로고    scopus 로고
    • Static and dynamic effects on vicinal scalar J couplings in proteins and peptides: A MD/DFT analysis
    • DOI 10.1021/ja001798p
    • DA Case C Scheurer R Bruschweiler 2000 Static and dynamic effects on vicinal scalar J couplings in proteins and peptides: a MD/DFT analysis J Am Chem Soc 122 42 10390 10397 10.1021/ja001798p (Pubitemid 30812114)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.42 , pp. 10390-10397
    • Case, D.A.1    Scheurer, C.2    Bruschweiler, R.3
  • 4
    • 0025856806 scopus 로고
    • Denatures states of proteins
    • 10.1146/annurev.bi.60.070191.004051
    • KA Dill D Shortle 1991 Denatures states of proteins Ann Rev Biochem 60 795 825 10.1146/annurev.bi.60.070191.004051
    • (1991) Ann Rev Biochem , vol.60 , pp. 795-825
    • Dill, K.A.1    Shortle, D.2
  • 5
    • 60349087841 scopus 로고    scopus 로고
    • Biophysical characterization of intrinsically disordered proteins
    • 10.1016/j.sbi.2008.12.004
    • D Eliezer 2009 Biophysical characterization of intrinsically disordered proteins Curr Opin Struct Biol 19 1 23 30 10.1016/j.sbi.2008.12.004
    • (2009) Curr Opin Struct Biol , vol.19 , Issue.1 , pp. 23-30
    • Eliezer, D.1
  • 6
    • 44949280676 scopus 로고
    • Band-selective radiofrequency pulses
    • H Geen R Freeman 1991 Band-selective radiofrequency pulses J Magn Reson 93 1 93 141
    • (1991) J Magn Reson , vol.93 , Issue.1 , pp. 93-141
    • Geen, H.1    Freeman, R.2
  • 7
    • 0000587142 scopus 로고
    • Interference between J-couplings and cross-relaxation in solution NMR spectroscopy: Consequences for macromolecular structure determination
    • 10.1021/ja00060a081
    • GS Harbison 1993 Interference between J-couplings and cross-relaxation in solution NMR spectroscopy: consequences for macromolecular structure determination J Am Chem Soc 115 7 3026 3027 10.1021/ja00060a081
    • (1993) J Am Chem Soc , vol.115 , Issue.7 , pp. 3026-3027
    • Harbison, G.S.1
  • 8
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • 10.1021/ja00052a088
    • LE Kay P Keifer T Saarinen 1992 Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity J Am Chem Soc 114 26 10663 10665 10.1021/ja00052a088
    • (1992) J Am Chem Soc , vol.114 , Issue.26 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 9
    • 0026711044 scopus 로고
    • Backbone dynamics of calcium-loaded calbindin D9k studied by 2-dimensional proton-detected N-15 NMR-spectroscopy
    • 10.1021/bi00135a017
    • J Kördel NJ Skelton M Akke AG Palmer WJ Chazin 1992 Backbone dynamics of calcium-loaded calbindin D9k studied by 2-dimensional proton-detected N-15 NMR-spectroscopy Biochemistry 31 20 4856 4866 10.1021/bi00135a017
    • (1992) Biochemistry , vol.31 , Issue.20 , pp. 4856-4866
    • Kördel, J.1    Skelton, N.J.2    Akke, M.3    Palmer, A.G.4    Chazin, W.J.5
  • 10
    • 0028545648 scopus 로고
    • Measurement of HN-Halpha J-couplings in calcium-free calmodulin using new 2D and 3D water flip-back methods
    • 10.1007/BF00398416
    • H Kuboniwa S Grzesiek F Delaglio A Bax 1994 Measurement of HN-Halpha J-couplings in calcium-free calmodulin using new 2D and 3D water flip-back methods J Biomol NMR 4 6 871 878 10.1007/BF00398416
    • (1994) J Biomol NMR , vol.4 , Issue.6 , pp. 871-878
    • Kuboniwa, H.1    Grzesiek, S.2    Delaglio, F.3    Bax, A.4
  • 11
    • 67349091665 scopus 로고    scopus 로고
    • 3D J-resolved NMR spectroscopy for unstructured polypeptides: Fast measurement of (3)J(HNH-alpha) coupling constants with outstanding spectral resolution
    • 10.1007/s10858-009-9313-3
    • C Lendel P Damberg 2009 3D J-resolved NMR spectroscopy for unstructured polypeptides: fast measurement of (3)J(HNH-alpha) coupling constants with outstanding spectral resolution J Biomol NMR 44 1 35 42 10.1007/s10858-009-9313- 3
    • (2009) J Biomol NMR , vol.44 , Issue.1 , pp. 35-42
    • Lendel, C.1    Damberg, P.2
  • 12
    • 33846913510 scopus 로고    scopus 로고
    • Atomic-level characterization of disordered protein ensembles
    • DOI 10.1016/j.sbi.2007.01.009, PII S0959440X07000103, Foldinf and Binding / Protein-Nucleic Interactions
    • T Mittag JD Forman-Kay 2007 Atomic-level characterization of disordered protein ensembles Curr Opin Struct Biol 17 1 3 14 10.1016/j.sbi.2007.01.009 (Pubitemid 46240819)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.1 , pp. 3-14
    • Mittag, T.1    Forman-Kay, J.D.2
  • 14
    • 50349090754 scopus 로고    scopus 로고
    • Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3
    • 10.1529/biophysj.107.126995
    • A Paz T Zeev-Ben-Mordehai E Sherman, et al. 2008 Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3 Biophys J 95 4 1928 1944 10.1529/biophysj.107. 126995
    • (2008) Biophys J , vol.95 , Issue.4 , pp. 1928-1944
    • Paz, A.1    Zeev-Ben-Mordehai, T.2    Sherman, E.3
  • 15
    • 0036038892 scopus 로고    scopus 로고
    • Cosine modulated HSQC: A rapid determination of (3)J(HNH alpha) scalar couplings in N-15-labeled proteins
    • 10.1006/jmre.2002.2538 2002JMagR.156.313P
    • A Petit SJF Vincent C Zwahlen 2002 Cosine modulated HSQC: a rapid determination of (3)J(HNH alpha) scalar couplings in N-15-labeled proteins J Magn Reson 156 2 313 317 10.1006/jmre.2002.2538 2002JMagR.156..313P
    • (2002) J Magn Reson , vol.156 , Issue.2 , pp. 313-317
    • Petit, A.1    Vincent, S.J.F.2    Zwahlen, C.3
  • 16
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR-spectroscopy of aqueous solutions
    • 10.1007/BF02192855
    • M Piotto V Saudek V Sklenar 1992 Gradient-tailored excitation for single-quantum NMR-spectroscopy of aqueous solutions J Biomol NMR 2 6 661 665 10.1007/BF02192855
    • (1992) J Biomol NMR , vol.2 , Issue.6 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 17
    • 0032132882 scopus 로고    scopus 로고
    • Rapid measurement of scalar three-bond H-1(N)-H-1(alpha) spin coupling constants in N-15-labelled proteins
    • 10.1023/A:1008293016073
    • H Ponstingl G Otting 1998 Rapid measurement of scalar three-bond H-1(N)-H-1(alpha) spin coupling constants in N-15-labelled proteins J Biomol NMR 12 2 319 324 10.1023/A:1008293016073
    • (1998) J Biomol NMR , vol.12 , Issue.2 , pp. 319-324
    • Ponstingl, H.1    Otting, G.2
  • 18
    • 0001697580 scopus 로고
    • New principles for the determination of coupling constants that largely suppresses differential relaxation effects
    • 10.1021/ja00146a027
    • A Rexroth P Schmidt S Szalma T Geppert H Schwalbe C Griesinger 1995 New principles for the determination of coupling constants that largely suppresses differential relaxation effects J Am Chem Soc 117 41 10389 10390 10.1021/ja00146a027
    • (1995) J Am Chem Soc , vol.117 , Issue.41 , pp. 10389-10390
    • Rexroth, A.1    Schmidt, P.2    Szalma, S.3    Geppert, T.4    Schwalbe, H.5    Griesinger, C.6
  • 19
    • 0029961647 scopus 로고    scopus 로고
    • Structural analysis of non-native states of proteins by NMR methods
    • DOI 10.1016/S0959-440X(96)80091-1
    • DR Shortle 1996 Structural analysis of non-native states of proteins by NMR methods Curr Opin Struct Biol 6 1 24 30 10.1016/S0959-440X(96)80091-1 (Pubitemid 26073941)
    • (1996) Current Opinion in Structural Biology , vol.6 , Issue.1 , pp. 24-30
    • Shortle, D.R.1
  • 20
    • 0026503169 scopus 로고
    • Proline cis-trans isomers in calbindin D9k observed by X-ray crystallography
    • 10.1016/0022-2836(92)90976-Q
    • LA Svensson E Thulin S Forsén 1992 Proline cis-trans isomers in calbindin D9k observed by X-ray crystallography J Mol Biol 223 3 601 606 10.1016/0022-2836(92)90976-Q
    • (1992) J Mol Biol , vol.223 , Issue.3 , pp. 601-606
    • Svensson, L.A.1    Thulin, E.2    Forsén, S.3
  • 21
    • 34547670259 scopus 로고    scopus 로고
    • Limits on variations in protein backbone dynamics from precise measurements of scalar couplings
    • DOI 10.1021/ja070324o
    • B Vogeli JF Ying A Grishaev A Bax 2007 Limits on variations in protein backbone dynamics from precise measurements of scalar couplings J Am Chem Soc 129 30 9377 9385 10.1021/ja070324o (Pubitemid 47218806)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.30 , pp. 9377-9385
    • Vogeli, B.1    Ying, J.2    Grishaev, A.3    Bax, A.4
  • 22
    • 12044259775 scopus 로고
    • Quantitative J correlation-a new approach for measuring homonuclear 3-bond J(HNHalpha) couplings-constants in N-15 enriched proteins
    • 10.1021/ja00070a024
    • GW Vuister A Bax 1993 Quantitative J correlation-a new approach for measuring homonuclear 3-bond J(HNHalpha) couplings-constants in N-15 enriched proteins J Am Chem Soc 115 17 7772 7777 10.1021/ja00070a024
    • (1993) J Am Chem Soc , vol.115 , Issue.17 , pp. 7772-7777
    • Vuister, G.W.1    Bax, A.2
  • 23
    • 0029879363 scopus 로고    scopus 로고
    • Determination of the backbone dihedral angles Φ in human ubiquitin from reparametrized empirical Karplus equations
    • DOI 10.1021/ja9535524
    • AC Wang A Bax 1996 Determination of the backbone dihedral angles phi in human ubiquitin from reparametrized empirical Karplus equations J Am Chem Soc 118 10 2483 2494 10.1021/ja9535524 (Pubitemid 26120929)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.10 , pp. 2483-2494
    • Wang, A.C.1    Bax, A.2
  • 24
    • 0037184476 scopus 로고    scopus 로고
    • Investigation of the neighboring residue effects on protein chemical shifts
    • DOI 10.1021/ja026811f
    • YJ Wang O Jardetzky 2002 Investigation of the neighboring residue effects on protein chemical shifts J Am Chem Soc 124 47 14075 14084 10.1021/ja026811f (Pubitemid 35386860)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.47 , pp. 14075-14084
    • Wang, Y.1    Jardetzky, O.2
  • 25
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life
    • DOI 10.1016/j.jmb.2004.02.002, PII S0022283604001482
    • JJ Ward JS Sodhi LJ McGuffin BF Buxton DT Jones 2004 Prediction and functional analysis of native disorder in proteins from the three kingdoms of life J Mol Biol 337 3 635 645 10.1016/j.jmb.2004.02.002 (Pubitemid 38326883)
    • (2004) Journal of Molecular Biology , vol.337 , Issue.3 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 26
    • 84888743437 scopus 로고    scopus 로고
    • Conformation and dynamics of nonnative states of proteins studied by NMR spectroscopy
    • J. Buchner T. Kiefhaber (eds). Wiley-VCH Weinheim. 10.1002/9783527619498. ch21
    • Wirmer J, Schlörb C, Schwalbe H (2005) Conformation and dynamics of nonnative states of proteins studied by NMR spectroscopy. In: Buchner J, Kiefhaber T (eds) Protein folding handbook part I. Wiley-VCH, Weinheim, pp 737-808
    • (2005) Protein Folding Handbook Part i , pp. 737-808
    • Wirmer, J.1    Schlörb, C.2    Schwalbe, H.3
  • 27
    • 0029181728 scopus 로고
    • H-1, C-13 and N-15 random coil NMR chemical-shifts of the common amino-acids .1. Investigations of nearest-neighbor effects
    • 10.1007/BF00227471
    • DS Wishart CG Bigam A Holm RS Hodges BD Sykes 1995 H-1, C-13 and N-15 random coil NMR chemical-shifts of the common amino-acids.1. Investigations of nearest-neighbor effects J Biomol NMR 5 1 67 81 10.1007/BF00227471
    • (1995) J Biomol NMR , vol.5 , Issue.1 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 28
    • 0032840124 scopus 로고    scopus 로고
    • Improved lineshape and sensitivity in the HNCO-family of triple resonance experiments
    • DOI 10.1023/A:1008381929212
    • D Yang LE Kay 1999 Improved lineshape and sensitivity in the HNCO-family of triple resonance experiments J Biomol NMR 14 3 273 276 10.1023/A: 1008381929212 (Pubitemid 29396485)
    • (1999) Journal of Biomolecular NMR , vol.14 , Issue.3 , pp. 273-276
    • Yang, D.1    Kay, L.E.2
  • 29
    • 0031451750 scopus 로고    scopus 로고
    • Chemical shift dispersion and secondary structure prediction in unfolded and partly folded proteins
    • DOI 10.1016/S0014-5793(97)01474-9, PII S0014579397014749
    • J Yao HJ Dyson PE Wright 1997 Chemical shift dispersion and secondary structure prediction in unfolded and partly folded proteins FEBS Lett 419 2-3 285 289 10.1016/S0014-5793(97)01474-9 (Pubitemid 28010828)
    • (1997) FEBS Letters , vol.419 , Issue.2-3 , pp. 285-289
    • Yao, J.1    Dyson, H.J.2    Wright, P.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.