메뉴 건너뛰기




Volumn 67, Issue 1, 2007, Pages 18-30

Probing nascent structures in peptides using natural abundance 13C NMR relaxation and reduced spectral density mapping

Author keywords

13C relaxation; Chemokines; Dynamics; HoxB1; ITAC; NMR; Peptides; SDF 1; vMIP II

Indexed keywords

CHEMOKINE; HOX PROTEIN; HOXB1 PROTEIN; MACROPHAGE INFLAMMATORY PROTEIN 2; PEPTIDE; STROMAL CELL DERIVED FACTOR 1; UNCLASSIFIED DRUG;

EID: 33847350241     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21294     Document Type: Article
Times cited : (7)

References (61)
  • 1
    • 0032972986 scopus 로고    scopus 로고
    • Is protein folding hierarchic? I. Local structure and peptide folding
    • Baldwin RL, Rose GD. Is protein folding hierarchic? I. Local structure and peptide folding. Trends Biochem Sci 1999;24:26-33.
    • (1999) Trends Biochem Sci , vol.24 , pp. 26-33
    • Baldwin, R.L.1    Rose, G.D.2
  • 2
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill KA. Dominant forces in protein folding. Biochemistry 1990;29:7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 3
    • 0030330918 scopus 로고    scopus 로고
    • Insights into protein folding from NMR
    • Dyson HJ, Wright PE. Insights into protein folding from NMR. Annu Rev Phys Chem 1996;47:369-395.
    • (1996) Annu Rev Phys Chem , vol.47 , pp. 369-395
    • Dyson, H.J.1    Wright, P.E.2
  • 4
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson HJ, Wright PE. Coupling of folding and binding for unstructured proteins. Curr Opin Struct Biol 2002;12:54-60.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 5
    • 0035793439 scopus 로고    scopus 로고
    • Structure/function of human herpesvirus-8 MIP-II (1-71) and the antagonist N-terminal segment (1-10)
    • Crump MP, Elisseeva E, Gong JH, Clark-Lewis I, Sykes BD. Structure/function of human herpesvirus-8 MIP-II (1-71) and the antagonist N-terminal segment (1-10). FEBS Lett 2001;489:171-175.
    • (2001) FEBS Lett , vol.489 , pp. 171-175
    • Crump, M.P.1    Elisseeva, E.2    Gong, J.H.3    Clark-Lewis, I.4    Sykes, B.D.5
  • 6
    • 0034282389 scopus 로고    scopus 로고
    • NMR studies of active N-terminal peptides of stromal cell-derived factor-1. Structural basis for receptor binding
    • Elisseeva EL, Slupsky CM, Crump MP, Clark-Lewis I, Sykes BD. NMR studies of active N-terminal peptides of stromal cell-derived factor-1. Structural basis for receptor binding. J Biol Chem 2000;275:26799-26805.
    • (2000) J Biol Chem , vol.275 , pp. 26799-26805
    • Elisseeva, E.L.1    Slupsky, C.M.2    Crump, M.P.3    Clark-Lewis, I.4    Sykes, B.D.5
  • 7
    • 0037459231 scopus 로고    scopus 로고
    • Unmasking ligand binding motifs: Identification of a chemokine receptor niotif by NMR studies of antagonist peptides
    • Booth V, Slupsky CM, Clark-Lewis I, Sykes BD. Unmasking ligand binding motifs: identification of a chemokine receptor niotif by NMR studies of antagonist peptides. J Mol Biol 2003;327:329-334.
    • (2003) J Mol Biol , vol.327 , pp. 329-334
    • Booth, V.1    Slupsky, C.M.2    Clark-Lewis, I.3    Sykes, B.D.4
  • 8
    • 0035019657 scopus 로고    scopus 로고
    • The HoxB1 hexapeptide is a prefolded domain: Implications for the Pbx1/Hox interaction
    • Slupsky CM, Sykes DB, Gay GL, Sykes BD. The HoxB1 hexapeptide is a prefolded domain: implications for the Pbx1/Hox interaction. Protein Sci 2001;10:1244-1253.
    • (2001) Protein Sci , vol.10 , pp. 1244-1253
    • Slupsky, C.M.1    Sykes, D.B.2    Gay, G.L.3    Sykes, B.D.4
  • 9
    • 14844361989 scopus 로고    scopus 로고
    • NMR studies of protein structure and dynamics
    • Kay LE. NMR studies of protein structure and dynamics. J Magn Reson 2005;173:193-207.
    • (2005) J Magn Reson , vol.173 , pp. 193-207
    • Kay, L.E.1
  • 10
    • 0037398803 scopus 로고    scopus 로고
    • New approaches to the dynamic interpretation and prediction of NMR relaxation data from proteins
    • Brüschweiler R. New approaches to the dynamic interpretation and prediction of NMR relaxation data from proteins. Curr Opin Struct Biol 2003;13:175-183.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 175-183
    • Brüschweiler, R.1
  • 12
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. I. Theory and range of validity
    • Lipari G, Szabo A. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. I. Theory and range of validity. J Am Chem Soc 1982;104:4546-4559.
    • (1982) J Am Chem Soc , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 13
    • 33845553743 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. II. Analysis of experimental results
    • Lipari G, Szabo A. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. II. Analysis of experimental results. J Am Chem Soc 1982;104:4559-4570.
    • (1982) J Am Chem Soc , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 14
    • 0027988297 scopus 로고
    • Backbone dynamics of a highly disordered 131 residue fragment of staphylococcal nuclease
    • Alexandrescu AT, Shortle D. Backbone dynamics of a highly disordered 131 residue fragment of staphylococcal nuclease. J Mol Biol 1994;242:527-546.
    • (1994) J Mol Biol , vol.242 , pp. 527-546
    • Alexandrescu, A.T.1    Shortle, D.2
  • 15
    • 0035742209 scopus 로고    scopus 로고
    • A new approach to visualizing spectral density functions and deriving motional correlation time distributions: Applications to an α-helix forming peptide and to a well-folded protein
    • Idiyatullin D, Daragan VA, Mayo KH. A new approach to visualizing spectral density functions and deriving motional correlation time distributions: applications to an α-helix forming peptide and to a well-folded protein. J Magn Reson 2001;152:132-148.
    • (2001) J Magn Reson , vol.152 , pp. 132-148
    • Idiyatullin, D.1    Daragan, V.A.2    Mayo, K.H.3
  • 16
    • 0029299006 scopus 로고
    • 13C NMR relaxation studies of molecular motion in peptide fragments from human transthyretin
    • 13C NMR relaxation studies of molecular motion in peptide fragments from human transthyretin. J Magn Reson Ser B 1995;107:95-106.
    • (1995) J Magn Reson Ser B , vol.107 , pp. 95-106
    • Jarvis, J.A.1    Craik, D.J.2
  • 17
    • 0029921063 scopus 로고    scopus 로고
    • 13C NMR relaxation study of heparin disaccharide interactions with tripeptides GRG and GKG
    • 13C NMR relaxation study of heparin disaccharide interactions with tripeptides GRG and GKG. Biochem J 1996;315:447-454.
    • (1996) Biochem J , vol.315 , pp. 447-454
    • Mikhailov, D.1    Mayo, K.H.2    Pervin, A.3    Linhardt, R.J.4
  • 18
    • 0026784152 scopus 로고
    • Mapping of the spectral densities of N-H bond motions in eglin c using heteronuclear relaxation experiments
    • Peng JW, Wagner G. Mapping of the spectral densities of N-H bond motions in eglin c using heteronuclear relaxation experiments. Biochemistry 1992;31:8571-8586.
    • (1992) Biochemistry , vol.31 , pp. 8571-8586
    • Peng, J.W.1    Wagner, G.2
  • 19
    • 0000660936 scopus 로고
    • Mapping of spectral density functions using heteronuclear NMR relaxation measurements
    • Peng JW, Wagner G. Mapping of spectral density functions using heteronuclear NMR relaxation measurements. J Magn Reson 1992;98:308-332.
    • (1992) J Magn Reson , vol.98 , pp. 308-332
    • Peng, J.W.1    Wagner, G.2
  • 20
    • 0029623152 scopus 로고
    • Frequency spectrum of NH bonds in eglin c from spectral density mapping at multiple fields
    • Peng JW, Wagner G. Frequency spectrum of NH bonds in eglin c from spectral density mapping at multiple fields. Biochemistry 1995;34:16733-16752.
    • (1995) Biochemistry , vol.34 , pp. 16733-16752
    • Peng, J.W.1    Wagner, G.2
  • 21
    • 0029872895 scopus 로고    scopus 로고
    • Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions
    • Lefèvre JF, Dayie KT, Peng JW, Wagner G. Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions. Biochemistry 1996;35:2674-2686.
    • (1996) Biochemistry , vol.35 , pp. 2674-2686
    • Lefèvre, J.F.1    Dayie, K.T.2    Peng, J.W.3    Wagner, G.4
  • 30
  • 31
    • 0032554612 scopus 로고    scopus 로고
    • 13C NMR spectroscopy
    • 13C NMR spectroscopy. Biochemistry 1998;37:5426-5438.
    • (1998) Biochemistry , vol.37 , pp. 5426-5438
    • Spielmann, H.P.1
  • 32
    • 0032508715 scopus 로고    scopus 로고
    • Solution structure and internal motion of a bioactive peptide derived from nerve growth factor
    • Beglova N, LeSauteur L, Ekiel I, Saragovi HU, Gehring K. Solution structure and internal motion of a bioactive peptide derived from nerve growth factor. J Biol Chem 1998;273:23652-23658.
    • (1998) J Biol Chem , vol.273 , pp. 23652-23658
    • Beglova, N.1    LeSauteur, L.2    Ekiel, I.3    Saragovi, H.U.4    Gehring, K.5
  • 35
    • 0028541223 scopus 로고
    • A test of the model-free formulas-effects of anisotropic rotational diffusion and dimerization
    • Schurr JM, Babcock HP, Fujimoto BS. A test of the model-free formulas-effects of anisotropic rotational diffusion and dimerization. J Magn Reson Ser B 1994;105:211-224.
    • (1994) J Magn Reson Ser B , vol.105 , pp. 211-224
    • Schurr, J.M.1    Babcock, H.P.2    Fujimoto, B.S.3
  • 38
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay LE, Keifer P, Saarinen T. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J Am Chem Soc 1992;114:10663-10665.
    • (1992) J Am Chem Soc , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 39
    • 44949276869 scopus 로고
    • Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy
    • Palmer AG, Cavanagh J, Wright PE, Rance M. Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy. J Magn Reson 1991;93:151-170.
    • (1991) J Magn Reson , vol.93 , pp. 151-170
    • Palmer, A.G.1    Cavanagh, J.2    Wright, P.E.3    Rance, M.4
  • 41
    • 48549112585 scopus 로고
    • Interference effects in the relaxation of a pair of unlike spin-1/2 nuclei
    • Goldman M. Interference effects in the relaxation of a pair of unlike spin-1/2 nuclei. J Magn Reson 1984;60:437-452.
    • (1984) J Magn Reson , vol.60 , pp. 437-452
    • Goldman, M.1
  • 42
    • 18844478967 scopus 로고    scopus 로고
    • Backbone and methyl dynamics of the regulatory domain of troponin C: Anisotropic rotational diffusion and contribution of conformational entropy to calcium affinity
    • Gagné SM, Tsuda S, Spyracopoulos L, Kay LE, Sykes BD. Backbone and methyl dynamics of the regulatory domain of troponin C: anisotropic rotational diffusion and contribution of conformational entropy to calcium affinity. J Mol Biol 1998;278:667-686.
    • (1998) J Mol Biol , vol.278 , pp. 667-686
    • Gagné, S.M.1    Tsuda, S.2    Spyracopoulos, L.3    Kay, L.E.4    Sykes, B.D.5
  • 46
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • Johnson BA, Blevins RA. NMRView: a computer program for the visualization and analysis of NMR data. J Biomol NMR 1994;4:603-604.
    • (1994) J Biomol NMR , vol.4 , pp. 603-604
    • Johnson, B.A.1    Blevins, R.A.2
  • 47
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common, amino acids. I. Investigations of nearest-neighbor effects
    • 15N random coil NMR chemical shifts of the common, amino acids. I. Investigations of nearest-neighbor effects. J Biomol NMR 1995;5:67-81.
    • (1995) J Biomol NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 48
    • 0029207339 scopus 로고
    • 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG
    • 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG. J Biomol NMR 1995;5:14-24.
    • (1995) J Biomol NMR , vol.5 , pp. 14-24
    • Merutka, G.1    Dyson, H.J.2    Wright, P.E.3
  • 49
    • 0025804130 scopus 로고
    • Large differences in the helix propensities of alanine and glycine
    • Chakrabartty A, Schellman JA, Baldwin RL. Large differences in the helix propensities of alanine and glycine. Nature. 1991;351:586-588.
    • (1991) Nature , vol.351 , pp. 586-588
    • Chakrabartty, A.1    Schellman, J.A.2    Baldwin, R.L.3
  • 51
    • 0002881831 scopus 로고
    • Measurement of relaxation time constants for methyl-groups by proton detected heteronuclear NMR-spectroscopy
    • Palmer AG, Wright PE, Ranee M. Measurement of relaxation time constants for methyl-groups by proton detected heteronuclear NMR-spectroscopy. Chem Phys Lett 1991;185:41-46.
    • (1991) Chem Phys Lett , vol.185 , pp. 41-46
    • Palmer, A.G.1    Wright, P.E.2    Ranee, M.3
  • 52
    • 0029099201 scopus 로고
    • Generating multiple conformations of flexible peptides in solution based on NMR nuclear overhauser effect data-application to desmopressin
    • Wang JJ, Hodges RS, Sykes BD. Generating multiple conformations of flexible peptides in solution based on NMR nuclear overhauser effect data-application to desmopressin. J Am Chem Soc 1995;117:8627-8634.
    • (1995) J Am Chem Soc , vol.117 , pp. 8627-8634
    • Wang, J.J.1    Hodges, R.S.2    Sykes, B.D.3
  • 53
    • 4344707281 scopus 로고    scopus 로고
    • Unfolded proteins and protein folding studied by NMR
    • Dyson HJ, Wright PE. Unfolded proteins and protein folding studied by NMR. Chem Rev 2004;104:3607-3622.
    • (2004) Chem Rev , vol.104 , pp. 3607-3622
    • Dyson, H.J.1    Wright, P.E.2
  • 56
    • 0028052661 scopus 로고
    • Influence of molecular motion on the accuracy of NMR derived distances-a molecular dynamics study of two solvated model peptides
    • Abseher R, Lüdemann S, Schreiber H, Steinhauser O. Influence of molecular motion on the accuracy of NMR derived distances-a molecular dynamics study of two solvated model peptides. J Am Chem Soc 1994;116:4006-4018.
    • (1994) J Am Chem Soc , vol.116 , pp. 4006-4018
    • Abseher, R.1    Lüdemann, S.2    Schreiber, H.3    Steinhauser, O.4
  • 58
    • 0031049285 scopus 로고    scopus 로고
    • Backbone and side-chain dynamics of residues in a partially folded β-sheet peptide from platelet factor-4
    • Daragan VA, Ilyina EE, Fields CG, Fields GB, Mayo KH. Backbone and side-chain dynamics of residues in a partially folded β-sheet peptide from platelet factor-4. Protein Sci 1997;6:355-363.
    • (1997) Protein Sci , vol.6 , pp. 355-363
    • Daragan, V.A.1    Ilyina, E.E.2    Fields, C.G.3    Fields, G.B.4    Mayo, K.H.5
  • 59
    • 0035940465 scopus 로고    scopus 로고
    • Temperature dependence of dynamics and thermodynamics of the regulatory domain of human cardiac troponin C
    • Spyracopoulos L, Lavigne P, Crump MP, Gagne SM, Kay CM, Sykes BD. Temperature dependence of dynamics and thermodynamics of the regulatory domain of human cardiac troponin C. Biochemistry 2001;40:12541-12551.
    • (2001) Biochemistry , vol.40 , pp. 12541-12551
    • Spyracopoulos, L.1    Lavigne, P.2    Crump, M.P.3    Gagne, S.M.4    Kay, C.M.5    Sykes, B.D.6
  • 60
    • 23944507043 scopus 로고    scopus 로고
    • NMR structures of anti-HIV D-peptides derived from the N-terminus of viral chemokine vMIP-II
    • Mori M, Liu DX, Kumar S, Huang ZW. NMR structures of anti-HIV D-peptides derived from the N-terminus of viral chemokine vMIP-II. Biochem Biophys Phys Res Commun 2005;335:651-658.
    • (2005) Biochem Biophys Phys Res Commun , vol.335 , pp. 651-658
    • Mori, M.1    Liu, D.X.2    Kumar, S.3    Huang, Z.W.4
  • 61
    • 84985715908 scopus 로고
    • NMR studies of the rates of proline cis-trans isomerization in oligopeptides
    • Grathwohl C, Wüthrich K. NMR studies of the rates of proline cis-trans isomerization in oligopeptides. Biopolymers 1981;20:2623-2633.
    • (1981) Biopolymers , vol.20 , pp. 2623-2633
    • Grathwohl, C.1    Wüthrich, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.