메뉴 건너뛰기




Volumn 5, Issue 4, 2010, Pages

Fast mapping of global protein folding states by multivariate NMR: A GPS for proteins

Author keywords

[No Author keywords available]

Indexed keywords

ACID; ALPHA LACTALBUMIN; DODECYL SULFATE SODIUM; HYDROGEN; LACTALBUMIN; SURFACTANT;

EID: 77956335380     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0010262     Document Type: Article
Times cited : (20)

References (32)
  • 1
    • 5044235050 scopus 로고    scopus 로고
    • Ten thousand interactions for the molecular biologist
    • Aloy P, Russell RB (2004) Ten thousand interactions for the molecular biologist. Nat Biotechnol 22: 1317-1321.
    • (2004) Nat Biotechnol , vol.22 , pp. 1317-1321
    • Aloy, P.1    Russell, R.B.2
  • 2
    • 27144530248 scopus 로고    scopus 로고
    • Towards a proteome-scale map of the human protein-protein interaction network
    • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, et al. (2005) Towards a proteome-scale map of the human protein-protein interaction network. Nature 437: 1173-1178.
    • (2005) Nature , vol.437 , pp. 1173-1178
    • Rual, J.F.1    Venkatesan, K.2    Hao, T.3    Hirozane-Kishikawa, T.4    Dricot, A.5
  • 4
    • 0000600340 scopus 로고
    • "General intelligence" objectively determined and measured
    • Spearman C (1904) "General intelligence" objectively determined and measured. American Journal of Psychology 15: 201-292.
    • (1904) American Journal of Psychology , vol.15 , pp. 201-292
    • Spearman, C.1
  • 5
    • 10444236348 scopus 로고    scopus 로고
    • The equilibrium unfolding of MerP characterized by multivariate analysis of 2D NMR data
    • Berglund A, Brorsson AC, Jonsson BH, Sethson I (2005) The equilibrium unfolding of MerP characterized by multivariate analysis of 2D NMR data. J Magn Reson 172: 24-30.
    • (2005) J Magn Reson , vol.172 , pp. 24-30
    • Berglund, A.1    Brorsson, A.C.2    Jonsson, B.H.3    Sethson, I.4
  • 6
    • 34848912277 scopus 로고    scopus 로고
    • Principal component analysis of the pH-dependent conformational transitions of bovine beta-lactoglobulin monitored by heteronuclear NMR
    • Sakurai K, Goto Y (2007) Principal component analysis of the pH-dependent conformational transitions of bovine beta-lactoglobulin monitored by heteronuclear NMR. Proc Natl Acad Sci USA 104: 15346-15351.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 15346-15351
    • Sakurai, K.1    Goto, Y.2
  • 7
    • 0030059690 scopus 로고    scopus 로고
    • The molten globule state of alpha-lactalbumin
    • Kuwajima K (1996) The molten globule state of alpha-lactalbumin. Faseb J 10: 102-109.
    • (1996) Faseb J , vol.10 , pp. 102-109
    • Kuwajima, K.1
  • 8
    • 0017178548 scopus 로고
    • Three-state denaturation of alpha-lactalbumin by guanidine hydrochloride
    • Kuwajima K, Nitta K, Yoneyama M, Sugai S (1976) Three-state denaturation of alpha-lactalbumin by guanidine hydrochloride. J Mol Biol 106: 359-373.
    • (1976) J Mol Biol , vol.106 , pp. 359-373
    • Kuwajima, K.1    Nitta, K.2    Yoneyama, M.3    Sugai, S.4
  • 9
    • 56049121413 scopus 로고    scopus 로고
    • Alpha-Lactalbumin is unfolded by all classes of surfactants but by different mechanisms
    • Otzen DE, Sehgal P, Westh P (2009) Alpha-Lactalbumin is unfolded by all classes of surfactants but by different mechanisms. J Colloid Interface Sci 329: 273-283.
    • (2009) J Colloid Interface Sci , vol.329 , pp. 273-283
    • Otzen, D.E.1    Sehgal, P.2    Westh, P.3
  • 11
    • 0027428001 scopus 로고
    • Conformational changes of alpha-lactalbumin and its fragment, Phe31-Ile59, induced by sodium dodecyl sulfate
    • Hamada S, Takeda K (1993) Conformational changes of alpha-lactalbumin and its fragment, Phe31-Ile59, induced by sodium dodecyl sulfate. J Protein Chem 12: 477-482.
    • (1993) J Protein Chem , vol.12 , pp. 477-482
    • Hamada, S.1    Takeda, K.2
  • 12
    • 0033794319 scopus 로고    scopus 로고
    • Random coil chemical shifts in acidic 8 M urea: Implementation of random coil shift data in NMRView
    • Schwarzinger S, Kroon GJ, Foss TR, Wright PE, Dyson HJ (2000) Random coil chemical shifts in acidic 8 M urea: implementation of random coil shift data in NMRView. J Biomol NMR 18: 43-48.
    • (2000) J Biomol NMR , vol.18 , pp. 43-48
    • Schwarzinger, S.1    Kroon, G.J.2    Foss, T.R.3    Wright, P.E.4    Dyson, H.J.5
  • 13
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart DS, Sykes BD, Richards FM (1992) The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31: 1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 14
    • 20344374426 scopus 로고    scopus 로고
    • Conformational flexibility of alpha-lactalbumin related to its membrane binding capacity
    • Halskau O, Underhaug J, Froystein NA, Martinez A (2005) Conformational flexibility of alpha-lactalbumin related to its membrane binding capacity. J Mol Biol 349: 1072-1086.
    • (2005) J Mol Biol , vol.349 , pp. 1072-1086
    • Halskau, O.1    Underhaug, J.2    Froystein, N.A.3    Martinez, A.4
  • 15
    • 0027536094 scopus 로고
    • Structure and dynamics of the acid-denatured molten globule state of alphalactalbumin: A two-dimensional NMR study
    • Alexandrescu AT, Evans PA, Pitkeathly M, Baum J, Dobson CM (1993) Structure and dynamics of the acid-denatured molten globule state of alphalactalbumin: a two-dimensional NMR study. Biochemistry 32: 1707-1718.
    • (1993) Biochemistry , vol.32 , pp. 1707-1718
    • Alexandrescu, A.T.1    Evans, P.A.2    Pitkeathly, M.3    Baum, J.4    Dobson, C.M.5
  • 16
    • 0022702283 scopus 로고
    • Ca2+-induced alteration in the unfolding behavior of alpha-lactalbumin
    • Ikeguchi M, Kuwajima K, Sugai S (1986) Ca2+-induced alteration in the unfolding behavior of alpha-lactalbumin. J Biochem 99: 1191-1201.
    • (1986) J Biochem , vol.99 , pp. 1191-1201
    • Ikeguchi, M.1    Kuwajima, K.2    Sugai, S.3
  • 17
    • 0034599720 scopus 로고    scopus 로고
    • Mutational analysis of the propensity for amyloid formation by a globular protein
    • Chiti F, Taddei N, Bucciantini M, White P, Ramponi G, et al. (2000) Mutational analysis of the propensity for amyloid formation by a globular protein. Embo J 19: 1441-1449.
    • (2000) Embo J , vol.19 , pp. 1441-1449
    • Chiti, F.1    Taddei, N.2    Bucciantini, M.3    White, P.4    Ramponi, G.5
  • 18
    • 0022255660 scopus 로고
    • Collagen fibril formation in the presence of sodium dodecyl sulphate
    • Dombi GW, Halsall HB (1985) Collagen fibril formation in the presence of sodium dodecyl sulphate. Biochem J 228: 551-556.
    • (1985) Biochem J , vol.228 , pp. 551-556
    • Dombi, G.W.1    Halsall, H.B.2
  • 20
    • 0037048671 scopus 로고    scopus 로고
    • Stimulation and inhibition of fibril formation by a peptide in the presence of different concentrations of SDS
    • Pertinhez TA, Bouchard M, Smith RA, Dobson CM, Smith LJ (2002) Stimulation and inhibition of fibril formation by a peptide in the presence of different concentrations of SDS. FEBS Lett 529: 193-197.
    • (2002) FEBS Lett , vol.529 , pp. 193-197
    • Pertinhez, T.A.1    Bouchard, M.2    Smith, R.A.3    Dobson, C.M.4    Smith, L.J.5
  • 21
    • 4644335370 scopus 로고    scopus 로고
    • Low concentrations of sodium dodecyl sulfate induce the extension of beta 2- microglobulin-related amyloid fibrils at a neutral pH
    • Yamamoto S, Hasegawa K, Yamaguchi I, Tsutsumi S, Kardos J, et al. (2004) Low concentrations of sodium dodecyl sulfate induce the extension of beta 2- microglobulin-related amyloid fibrils at a neutral pH. Biochemistry 43: 11075-11082.
    • (2004) Biochemistry , vol.43 , pp. 11075-11082
    • Yamamoto, S.1    Hasegawa, K.2    Yamaguchi, I.3    Tsutsumi, S.4    Kardos, J.5
  • 22
    • 0033004311 scopus 로고    scopus 로고
    • Rapid collapse and slow structural reorganisation during the refolding of bovine alphalactalbumin
    • Forge V, Wijesinha RT, Balbach J, Brew K, Robinson CV, et al. (1999) Rapid collapse and slow structural reorganisation during the refolding of bovine alphalactalbumin. J Mol Biol 288: 673-688.
    • (1999) J Mol Biol , vol.288 , pp. 673-688
    • Forge, V.1    Wijesinha, R.T.2    Balbach, J.3    Brew, K.4    Robinson, C.V.5
  • 23
    • 0028009873 scopus 로고
    • Characterization of a trifluoroethanol-induced partially folded state of alpha-lactalbumin
    • Alexandrescu AT, Ng YL, Dobson CM (1994) Characterization of a trifluoroethanol-induced partially folded state of alpha-lactalbumin. J Mol Biol 235: 587-599.
    • (1994) J Mol Biol , vol.235 , pp. 587-599
    • Alexandrescu, A.T.1    Ng, Y.L.2    Dobson, C.M.3
  • 24
    • 33847302979 scopus 로고    scopus 로고
    • Ex situ NMR in highly homogeneous fields: 1H spectroscopy
    • Perlo J, Casanova F, Blumich B (2007) Ex situ NMR in highly homogeneous fields: 1H spectroscopy. Science 315: 1110-1112.
    • (2007) Science , vol.315 , pp. 1110-1112
    • Perlo, J.1    Casanova, F.2    Blumich, B.3
  • 25
    • 0033593529 scopus 로고    scopus 로고
    • Effect of the extra n-terminal methionine residue on the stability and folding of recombinant alpha-lactalbumin expressed in Escherichia coli
    • Chaudhuri TK, Horii K, Yoda T, Arai M, Nagata S, et al. (1999) Effect of the extra n-terminal methionine residue on the stability and folding of recombinant alpha-lactalbumin expressed in Escherichia coli. J Mol Biol 285: 1179-1194.
    • (1999) J Mol Biol , vol.285 , pp. 1179-1194
    • Chaudhuri, T.K.1    Horii, K.2    Yoda, T.3    Arai, M.4    Nagata, S.5
  • 26
    • 0029860435 scopus 로고    scopus 로고
    • Protein folding monitored at individual residues during a two-dimensional NMR experiment
    • Balbach J, Forge V, Lau WS, van Nuland NA, Brew K, et al. (1996) Protein folding monitored at individual residues during a two-dimensional NMR experiment. Science 274: 1161-1163.
    • (1996) Science , vol.274 , pp. 1161-1163
    • Balbach, J.1    Forge, V.2    Lau, W.S.3    van Nuland, N.A.4    Brew, K.5
  • 28
    • 34547463005 scopus 로고    scopus 로고
    • Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy
    • Schanda P, Forge V, Brutscher B (2007) Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy. Proc Natl Acad Sci USA 104: 11257-11262.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 11257-11262
    • Schanda, P.1    Forge, V.2    Brutscher, B.3
  • 29
    • 42249096940 scopus 로고    scopus 로고
    • Conserved folding pathways of alpha-lactalbumin and lysozyme revealed by kinetic CD, fluorescence, NMR, and interrupted refolding experiments
    • Schlepckow K, Wirmer J, Bachmann A, Kiefhaber T, Schwalbe H (2008) Conserved folding pathways of alpha-lactalbumin and lysozyme revealed by kinetic CD, fluorescence, NMR, and interrupted refolding experiments. J Mol Biol 378: 686-698.
    • (2008) J Mol Biol , vol.378 , pp. 686-698
    • Schlepckow, K.1    Wirmer, J.2    Bachmann, A.3    Kiefhaber, T.4    Schwalbe, H.5
  • 30
    • 0029001090 scopus 로고
    • Direct NMR evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A
    • Klefhaber T, Labhardt AM, Baldwin RL (1995) Direct NMR evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A. Nature 375: 513-515.
    • (1995) Nature , vol.375 , pp. 513-515
    • Klefhaber, T.1    Labhardt, A.M.2    Baldwin, R.L.3
  • 31
    • 0034823890 scopus 로고    scopus 로고
    • Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor
    • Mayer M, Meyer B (2001) Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor. J Am Chem Soc 123: 6108-6117.
    • (2001) J Am Chem Soc , vol.123 , pp. 6108-6117
    • Mayer, M.1    Meyer, B.2
  • 32
    • 0015909087 scopus 로고
    • Nuclear magnetic resonance studies of the interaction of peptides and hormones with bovine neurophysin
    • Balaram P, Bothner-By AA, Breslow E (1973) Nuclear magnetic resonance studies of the interaction of peptides and hormones with bovine neurophysin. Biochemistry 12: 4695-4704.
    • (1973) Biochemistry , vol.12 , pp. 4695-4704
    • Balaram, P.1    Bothner-By, A.A.2    Breslow, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.