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Volumn 895, Issue , 2012, Pages 361-386

Monitoring structural transitions in IDPs by site-directed spin labeling EPR spectroscopy

Author keywords

Electron paramagnetic resonance spectroscopy; Induced folding; Intrinsically disordered proteins; MTSL; Nitroxide radical; SDSL EPR; Site directed spin labeling; Spin labels; Spin probes; Structural transitions

Indexed keywords

CYSTEINE; HYBRID PROTEIN; NITROGEN OXIDE; NITROXYL; SUCROSE; TRIFLUOROETHANOL;

EID: 84865332732     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-61779-927-3_21     Document Type: Article
Times cited : (15)

References (44)
  • 1
    • 0000991119 scopus 로고    scopus 로고
    • Site-directed spinlabeling of membrane proteins and peptidemembrane interactions
    • Berliner L (ed) Plenum Press, New York
    • Feix JB, Klug CS (1998) Site-directed spinlabeling of membrane proteins and peptidemembrane interactions. In: Berliner L (ed) Biological magnetic resonance. Plenum Press, New York
    • (1998) Biological Magnetic Resonance
    • Feix, J.B.1    Klug, C.S.2
  • 4
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • Hubbell WL, Cafiso DS, Altenbach C (2000) Identifying conformational changes with site-directed spin labeling. Nat Struct Biol 7 (9):735-739
    • (2000) Nat Struct Biol , vol.7 , Issue.9 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 5
    • 0035235377 scopus 로고    scopus 로고
    • Use of EPR spectroscopy to study macromolecular structure and function
    • Biswas R, Kuhne H, Brudvig GW, Gopalan V (2001) Use of EPR spectroscopy to study macromolecular structure and function. Sci Prog 84(Pt 1):45-67
    • (2001) Sci Prog , vol.84 , Issue.PART 1 , pp. 45-67
    • Biswas, R.1    Kuhne, H.2    Brudvig, G.W.3    Gopalan, V.4
  • 6
    • 0036606899 scopus 로고    scopus 로고
    • A new spin on protein dynamics
    • Columbus L, Hubbell WL (2002) A new spin on protein dynamics. Trends Biochem Sci 27 (6):288-295
    • (2002) Trends Biochem Sci , vol.27 , Issue.6 , pp. 288-295
    • Columbus, L.1    Hubbell, W.L.2
  • 7
    • 0037285444 scopus 로고    scopus 로고
    • Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide crosslinking
    • Hubbell WL, Altenbach C, Hubbell CM, Khorana HG (2003) Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide crosslinking. Adv Protein Chem 63:243-290
    • (2003) Adv Protein Chem , vol.63 , pp. 243-290
    • Hubbell, W.L.1    Altenbach, C.2    Hubbell, C.M.3    Khorana, H.G.4
  • 8
    • 33749041288 scopus 로고    scopus 로고
    • Recent advances and applications of site-directed spin labeling
    • Fanucci GE, Cafiso DS (2006) Recent advances and applications of site-directed spin labeling. Curr Opin Struct Biol 16(5):644-653
    • (2006) Curr Opin Struct Biol , vol.16 , Issue.5 , pp. 644-653
    • Fanucci, G.E.1    Cafiso, D.S.2
  • 10
    • 0024974071 scopus 로고
    • Structural studies on transmembrane proteins. 2. Spin labeling of bacteriorhodopsin mutants at unique cysteines
    • Altenbach C, Flitsch SL, Khorana HG, Hubbell WL (1989) Structural studies on transmembrane proteins. 2. Spin labeling of bacteriorhodopsin mutants at unique cysteines. Biochemistry 28(19):7806-7812
    • (1989) Biochemistry , vol.28 , Issue.19 , pp. 7806-7812
    • Altenbach, C.1    Flitsch, S.L.2    Khorana, H.G.3    Hubbell, W.L.4
  • 11
    • 0025346254 scopus 로고
    • Transmembrane protein-structure: Spin labeling of bacteriorhodopsin mutants
    • Altenbach C, Marti T, Khorana HG, Hubbell WL (1990) Transmembrane protein-structure: spin labeling of bacteriorhodopsin mutants. Science 248(4959):1088-1092
    • (1990) Science , vol.248 , Issue.4959 , pp. 1088-1092
    • Altenbach, C.1    Marti, T.2    Khorana, H.G.3    Hubbell, W.L.4
  • 12
    • 33751289801 scopus 로고    scopus 로고
    • Assessing induced folding of an intrinsically disordered protein by site-directed spinlabeling EPR spectroscopy
    • Morin B, Bourhis JM, Belle V, Woudstra M, Carrière F, Guigliarelli B, Fournel A, Longhi S (2006) Assessing induced folding of an intrinsically disordered protein by site-directed spinlabeling EPR spectroscopy. J Phys Chem B 110 (41):20596-20608
    • (2006) J Phys Chem B , vol.110 , Issue.41 , pp. 20596-20608
    • Morin, B.1    Bourhis, J.M.2    Belle, V.3    Woudstra, M.4    Carrière, F.5    Guigliarelli, B.6    Fournel, A.7    Longhi, S.8
  • 13
    • 58149279796 scopus 로고    scopus 로고
    • Mapping alpha-helical induced folding within the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by site-directed spin-labeling EPR spectroscopy
    • Belle V, Rouger S, Costanzo S, Liquiere E, Strancar J, Guigliarelli B, Fournel A, Longhi S (2008) Mapping alpha-helical induced folding within the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by site-directed spin-labeling EPR spectroscopy. Proteins 73(4):973-988
    • (2008) Proteins , vol.73 , Issue.4 , pp. 973-988
    • Belle, V.1    Rouger, S.2    Costanzo, S.3    Liquiere, E.4    Strancar, J.5    Guigliarelli, B.6    Fournel, A.7    Longhi, S.8
  • 14
    • 78650772151 scopus 로고    scopus 로고
    • Characterization of the disordered-to-alpha-helical transition of IA by SDSL-EPR spectroscopy
    • Pirman NL, Milshteyn E, Galiano L, Hewlett JC, Fanucci GE (2011) Characterization of the disordered-to-alpha-helical transition of IA by SDSL-EPR spectroscopy. Protein Sci 20 (1):150-159
    • (2011) Protein Sci , vol.20 , Issue.1 , pp. 150-159
    • Pirman, N.L.1    Milshteyn, E.2    Galiano, L.3    Hewlett, J.C.4    Fanucci, G.E.5
  • 15
    • 0034132251 scopus 로고    scopus 로고
    • Dead-time free measurement of dipole-dipole interactions between electron spins
    • Pannier M, Veit S, Godt A, Jeschke G, Spiess HW (2000) Dead-time free measurement of dipole-dipole interactions between electron spins. J Magn Reson 142(2):331-340
    • (2000) J Magn Reson , vol.142 , Issue.2 , pp. 331-340
    • Pannier, M.1    Veit, S.2    Godt, A.3    Jeschke, G.4    Spiess, H.W.5
  • 16
    • 0346732181 scopus 로고    scopus 로고
    • Co-conformational distribution of nanosized [2]catenanes determined by pulse EPR measurements
    • Jeschke G, Godt A (2003) Co-conformational distribution of nanosized [2]catenanes determined by pulse EPR measurements. Chemphyschem 4(12):1328-1334
    • (2003) Chemphyschem , vol.4 , Issue.12 , pp. 1328-1334
    • Jeschke, G.1    Godt, A.2
  • 18
    • 1942487282 scopus 로고    scopus 로고
    • Interresidual distance determination by four-pulse double electronelectron resonance in an integral membrane protein: The Na +proline transporter PutP of Escherichia coli
    • Jeschke G, Wegener C, Nietschke M, Jung H, Steinhoff HJ (2004) Interresidual distance determination by four-pulse double electronelectron resonance in an integral membrane protein: the Na +proline transporter PutP of Escherichia coli. Biophys J 86(4):2551-2557
    • (2004) Biophys J , vol.86 , Issue.4 , pp. 2551-2557
    • Jeschke, G.1    Wegener, C.2    Nietschke, M.3    Jung, H.4    Steinhoff, H.J.5
  • 19
    • 24944546549 scopus 로고    scopus 로고
    • Coupled folding and binding with alpha-helix-forming molecular recognition elements
    • Oldfield CJ, Cheng Y, Cortese MS, Romero P, Uversky VN, Dunker AK (2005) Coupled folding and binding with alpha-helix-forming molecular recognition elements. Biochemistry 44(37):12454-12470
    • (2005) Biochemistry , vol.44 , Issue.37 , pp. 12454-12470
    • Oldfield, C.J.1    Cheng, Y.2    Cortese, M.S.3    Romero, P.4    Uversky, V.N.5    Dunker, A.K.6
  • 22
    • 34249695447 scopus 로고    scopus 로고
    • Local structural disorder imparts plasticity on linear motifs
    • Fuxreiter M, Tompa P, Simon I (2007) Local structural disorder imparts plasticity on linear motifs. Bioinformatics 23(8):950-956
    • (2007) Bioinformatics , vol.23 , Issue.8 , pp. 950-956
    • Fuxreiter, M.1    Tompa, P.2    Simon, I.3
  • 23
    • 79953780789 scopus 로고    scopus 로고
    • Probing structural transitions in both structured and disordered proteins by site-directed spin-labeling EPR spectroscopy
    • Longhi S, Belle V, Fournel A, Guigliarelli B, Carrière F (2011) Probing structural transitions in both structured and disordered proteins by site-directed spin-labeling EPR spectroscopy. J Pept Sci 17(5):315-328
    • (2011) J Pept Sci , vol.17 , Issue.5 , pp. 315-328
    • Longhi, S.1    Belle, V.2    Fournel, A.3    Guigliarelli, B.4    Carrière, F.5
  • 25
    • 70349996473 scopus 로고    scopus 로고
    • ANCHOR: Web server for predicting protein binding regions in disordered proteins
    • Dosztanyi Z, Meszaros B, Simon I (2009) ANCHOR: web server for predicting protein binding regions in disordered proteins. Bioinformatics 25(20):2745-2746
    • (2009) Bioinformatics , vol.25 , Issue.20 , pp. 2745-2746
    • Dosztanyi, Z.1    Meszaros, B.2    Simon, I.3
  • 28
    • 33748258328 scopus 로고    scopus 로고
    • A practical overview of protein disorder prediction methods
    • Ferron F, Longhi S, Canard B, Karlin D (2006) A practical overview of protein disorder prediction methods. Proteins 65(1):1-14
    • (2006) Proteins , vol.65 , Issue.1 , pp. 1-14
    • Ferron, F.1    Longhi, S.2    Canard, B.3    Karlin, D.4
  • 29
    • 34247640113 scopus 로고    scopus 로고
    • Predicting protein disorder and induced folding: From theoretical principles to practical applications
    • Bourhis JM, Canard B, Longhi S (2007) Predicting protein disorder and induced folding: from theoretical principles to practical applications. Curr Protein Pept Sci 8(2):135-149
    • (2007) Curr Protein Pept Sci , vol.8 , Issue.2 , pp. 135-149
    • Bourhis, J.M.1    Canard, B.2    Longhi, S.3
  • 30
    • 77952780789 scopus 로고    scopus 로고
    • Conformational disorder
    • Longhi S (2010) Conformational disorder. Methods Mol Biol 609:307-325
    • (2010) Methods Mol Biol , vol.609 , pp. 307-325
    • Longhi, S.1
  • 31
    • 77955399035 scopus 로고    scopus 로고
    • Structural disorder within Henipavirus nucleoprotein and phosphoprotein: From predictions to experimental assessment
    • Habchi J, Mamelli L, Darbon H, Longhi S (2010) Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. PLoS One 5(7):e11684
    • (2010) PLoS One , vol.5 , Issue.7
    • Habchi, J.1    Mamelli, L.2    Darbon, H.3    Longhi, S.4
  • 33
    • 34547925579 scopus 로고    scopus 로고
    • Expression in Escherichia coli, refolding and crystallization of Aspergillus niger feruloyl esterase A using a serial factorial approach
    • Benoit I, Coutard B, Oubelaid R, Asther M, Bignon C (2007) Expression in Escherichia coli, refolding and crystallization of Aspergillus niger feruloyl esterase A using a serial factorial approach. Protein Expr Purif 55(1):166-174
    • (2007) Protein Expr Purif , vol.55 , Issue.1 , pp. 166-174
    • Benoit, I.1    Coutard, B.2    Oubelaid, R.3    Asther, M.4    Bignon, C.5
  • 35
    • 0032574795 scopus 로고    scopus 로고
    • Transcriptional activatorcoactivator recognition: Nascent folding of a kinase-inducible transactivation domain predicts its structure on coactivator binding
    • Hua QX, Jia WH, Bullock BP, Habener JF, Weiss MA (1998) Transcriptional activatorcoactivator recognition: nascent folding of a kinase-inducible transactivation domain predicts its structure on coactivator binding. Biochemistry 37(17):5858-5866
    • (1998) Biochemistry , vol.37 , Issue.17 , pp. 5858-5866
    • Hua, Q.X.1    Jia, W.H.2    Bullock, B.P.3    Habener, J.F.4    Weiss, M.A.5
  • 36
    • 0027522642 scopus 로고
    • The acidic activation domains of the GCN4 and GAL4 proteins are not alpha helical but form beta sheets
    • Van Hoy M, Leuther KK, Kodadek T, Johnston SA (1993) The acidic activation domains of the GCN4 and GAL4 proteins are not alpha helical but form beta sheets. Cell 72 (4):587-594
    • (1993) Cell , vol.72 , Issue.4 , pp. 587-594
    • Van Hoy, M.1    Leuther, K.K.2    Kodadek, T.3    Johnston, S.A.4
  • 37
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore L, Wallace BA (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res 32(Web Server issue):W668-W673
    • (2004) Nucleic Acids Res , vol.32 , Issue.WEB SERVER ISSUE
    • Whitmore, L.1    Wallace, B.A.2
  • 38
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • Whitmore L, Wallace BA (2008) Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 89(5):392-400
    • (2008) Biopolymers , vol.89 , Issue.5 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 40
    • 0030937861 scopus 로고    scopus 로고
    • Kinetics and motional dynamics of spin-labeled yeast iso-1-cytochrome c: 1. Stopped-flow electron paramagnetic resonance as a probe for protein folding/unfolding of the C-terminal helix spin-labeled at cysteine 102
    • Qu K, Vaughn JL, Sienkiewicz A, Scholes CP, Fetrow JS (1997) Kinetics and motional dynamics of spin-labeled yeast iso-1-cytochrome c: 1. Stopped-flow electron paramagnetic resonance as a probe for protein folding/unfolding of the C-terminal helix spin-labeled at cysteine 102. Biochemistry 36 (10):2884-2897
    • (1997) Biochemistry , vol.36 , Issue.10 , pp. 2884-2897
    • Qu, K.1    Vaughn, J.L.2    Sienkiewicz, A.3    Scholes, C.P.4    Fetrow, J.S.5
  • 41
    • 84857379330 scopus 로고
    • An ESR study of anisotropic rotational reorientation and slow tumbling in liquid and frozen media
    • Goldman A, Bruno GV, Polnaszek CF, Freed JH (1972) An ESR study of anisotropic rotational reorientation and slow tumbling in liquid and frozen media. J Chem Phys 56:716-735
    • (1972) J Chem Phys , vol.56 , pp. 716-735
    • Goldman, A.1    Bruno, G.V.2    Polnaszek, C.F.3    Freed, J.H.4
  • 43
    • 0029905422 scopus 로고    scopus 로고
    • Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics
    • McHaourab HS, Lietzow MA, Hideg K, Hubbell WL (1996) Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics. Biochemistry 35 (24):7692-7704
    • (1996) Biochemistry , vol.35 , Issue.24 , pp. 7692-7704
    • McHaourab, H.S.1    Lietzow, M.A.2    Hideg, K.3    Hubbell, W.L.4
  • 44
    • 28844486080 scopus 로고    scopus 로고
    • EasySpin, a comprehensive software package for spectral simulation and analysis in EPR
    • Stoll S, Schweiger A (2006) EasySpin, a comprehensive software package for spectral simulation and analysis in EPR. J Magn Reson 178 (1):42-55
    • (2006) J Magn Reson , vol.178 , Issue.1 , pp. 42-55
    • Stoll, S.1    Schweiger, A.2


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