메뉴 건너뛰기




Volumn 116, Issue 1, 2012, Pages 520-531

Structural and dynamical insights into the molten-globule form of ovalbumin

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS;

EID: 84855833470     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp208416d     Document Type: Article
Times cited : (43)

References (41)
  • 1
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn, O. B. Molten globule and protein folding Adv. Protein Chem. 1995, 47, 83-229
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 2
    • 36749078792 scopus 로고    scopus 로고
    • Folding vs aggregation: Polypeptide conformations on competing pathways
    • Jahn, T. R.; Radford, S. E. Folding vs aggregation: Polypeptide conformations on competing pathways Arch. Biochem. Biophys. 2008, 469, 100-117
    • (2008) Arch. Biochem. Biophys. , vol.469 , pp. 100-117
    • Jahn, T.R.1    Radford, S.E.2
  • 3
    • 46549084254 scopus 로고    scopus 로고
    • Protein misfolding and disease: From the test tube to the organism
    • Luheshi, L. M.; Crowther, D. C.; Dobson, C. M. Protein misfolding and disease: From the test tube to the organism Curr. Opin. Chem. Biol. 2008, 12, 25-31
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 25-31
    • Luheshi, L.M.1    Crowther, D.C.2    Dobson, C.M.3
  • 4
    • 67650713938 scopus 로고    scopus 로고
    • Conformational pathology of the serpins: Themes, variations and therapeutic strategies
    • Gooptu, B.; Lomas, D. A. Conformational pathology of the serpins: Themes, variations and therapeutic strategies Annu. Rev. Biochem. 2009, 78, 147-176
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 147-176
    • Gooptu, B.1    Lomas, D.A.2
  • 6
    • 0025742788 scopus 로고
    • Serpin tertiary structure transformation
    • Stein, P.; Chothia, C. Serpin tertiary structure transformation J. Mol. Biol. 1991, 221, 615-621
    • (1991) J. Mol. Biol. , vol.221 , pp. 615-621
    • Stein, P.1    Chothia, C.2
  • 7
    • 0028873168 scopus 로고
    • Recent advances in the understanding of egg white protein functionality
    • Mine, Y. Recent advances in the understanding of egg white protein functionality Trends Food Sci. Technol. 1995, 6, 225-232
    • (1995) Trends Food Sci. Technol. , vol.6 , pp. 225-232
    • Mine, Y.1
  • 9
    • 0025949027 scopus 로고
    • Crystal structure of uncleaved ovalbumin at l.95 Å resolution
    • Stein, P. E.; Leslie, A. G. W.; Finch, J. T.; Carrell, R. W. Crystal structure of uncleaved ovalbumin at l.95 Å resolution J. Mol. Biol. 1991, 221, 941-959
    • (1991) J. Mol. Biol. , vol.221 , pp. 941-959
    • Stein, P.E.1    Leslie, A.G.W.2    Finch, J.T.3    Carrell, R.W.4
  • 10
    • 0027393310 scopus 로고
    • The ovalbumin family of serpin proteins
    • Donnell, E. R.-O. The ovalbumin family of serpin proteins FEBS Lett. 1993, 315, 105-108
    • (1993) FEBS Lett. , vol.315 , pp. 105-108
    • Donnell, E.R.-O.1
  • 11
    • 0023972819 scopus 로고
    • Conformational changes in ovalbumin at acid pH
    • Koseki, T.; Kitabatake, N.; Doi, E. Conformational changes in ovalbumin at acid pH J. Biochem. 1988, 103, 425-430
    • (1988) J. Biochem. , vol.103 , pp. 425-430
    • Koseki, T.1    Kitabatake, N.2    Doi, E.3
  • 12
    • 0030803337 scopus 로고    scopus 로고
    • Highly ordered molten globule-like state of ovalbumin at acidic pH: Native-like fragmentation by protease and selective modification of Cys367 with dithiopyridine
    • Tatsumi, E.; Hirose, M. Highly ordered molten globule-like state of ovalbumin at acidic pH: Native-like fragmentation by protease and selective modification of Cys367 with dithiopyridine J. Biochem. 1997, 122, 300-308
    • (1997) J. Biochem. , vol.122 , pp. 300-308
    • Tatsumi, E.1    Hirose, M.2
  • 13
    • 0032169568 scopus 로고    scopus 로고
    • Conformational state of ovalbumin at acidic pH as evaluated by a novel approach utilizing intrachain sulfhydryl-mixed disulfide exchange reactions
    • Tatsumi, E.; Yoshimatsu, D.; Hirose, M. Conformational state of ovalbumin at acidic pH as evaluated by a novel approach utilizing intrachain sulfhydryl-mixed disulfide exchange reactions Biochemistry 1998, 37, 12351-12359
    • (1998) Biochemistry , vol.37 , pp. 12351-12359
    • Tatsumi, E.1    Yoshimatsu, D.2    Hirose, M.3
  • 15
    • 84906359335 scopus 로고    scopus 로고
    • CDNN: CD Spectra Deconvolution, Version 2.1
    • Böhm., G. CDNN: CD Spectra Deconvolution, Version 2.1, 1997.
    • (1997)
    • Böhm, G.1
  • 16
    • 77954495192 scopus 로고    scopus 로고
    • Fluorescence dynamics of double and single stranded DNA bound to histone and micellar surfaces
    • Goel, T.; Mukherjee, T.; Rao, B. J.; Krishnamoorthy, G. Fluorescence dynamics of double and single stranded DNA bound to histone and micellar surfaces J. Phys. Chem. B 2010, 114, 8986-8993
    • (2010) J. Phys. Chem. B , vol.114 , pp. 8986-8993
    • Goel, T.1    Mukherjee, T.2    Rao, B.J.3    Krishnamoorthy, G.4
  • 18
    • 79953777946 scopus 로고    scopus 로고
    • PH-Induced conformational isomerization of bovine serum albumin studied by extrinsic and intrinsic protein fluorescence
    • Bhattacharya, M.; Jain, N.; Bhasne, K.; Kumari, V.; Mukhopadhyay, S. pH-Induced conformational isomerization of bovine serum albumin studied by extrinsic and intrinsic protein fluorescence J. Fluoresc. 2011, 21, 1083-1090
    • (2011) J. Fluoresc. , vol.21 , pp. 1083-1090
    • Bhattacharya, M.1    Jain, N.2    Bhasne, K.3    Kumari, V.4    Mukhopadhyay, S.5
  • 19
    • 0013913906 scopus 로고
    • Cooperative effects in binding by bovine serum albumin I: The binding of 1-anilino-8-naphthalenesulfonate fluorimetric titrations
    • Daniel, E.; Weber, G. Cooperative effects in binding by bovine serum albumin I: The binding of 1-anilino-8-naphthalenesulfonate fluorimetric titrations Biochemistry 1966, 5, 1893-1900
    • (1966) Biochemistry , vol.5 , pp. 1893-1900
    • Daniel, E.1    Weber, G.2
  • 20
    • 33645968089 scopus 로고    scopus 로고
    • Molten globule formation in apomyoglobin monitored by the fluorescent probe Nile Red
    • Polverini, E.; Cugini, G.; Annoni, F.; Abbruzzetti, S.; Viappiani, C.; Gensch, T. Molten globule formation in apomyoglobin monitored by the fluorescent probe Nile Red Biochemistry 2006, 45, 5111-5121
    • (2006) Biochemistry , vol.45 , pp. 5111-5121
    • Polverini, E.1    Cugini, G.2    Annoni, F.3    Abbruzzetti, S.4    Viappiani, C.5    Gensch, T.6
  • 21
    • 0023476453 scopus 로고
    • Nile red as a polarity-sensitive fluorescent probe of hydrophobic protein surfaces
    • Sackett, D. L.; Wolff, J. Nile red as a polarity-sensitive fluorescent probe of hydrophobic protein surfaces Anal. Biochem. 1987, 167, 228-234
    • (1987) Anal. Biochem. , vol.167 , pp. 228-234
    • Sackett, D.L.1    Wolff, J.2
  • 22
    • 0036199841 scopus 로고    scopus 로고
    • Transient exposure of hydrophobic surface in the photoactive yellow protein monitored with Nile red
    • Hendriks, J.; Gensch, T.; Hviid, L.; van der Horst, M. A.; Hellingwerf, K. J.; van Thor, J. J. Transient exposure of hydrophobic surface in the photoactive yellow protein monitored with Nile red Biophys. J. 2002, 82, 1632-1643
    • (2002) Biophys. J. , vol.82 , pp. 1632-1643
    • Hendriks, J.1    Gensch, T.2    Hviid, L.3    Van Der Horst, M.A.4    Hellingwerf, K.J.5    Van Thor, J.J.6
  • 24
    • 11144223201 scopus 로고    scopus 로고
    • Exploring protein folding ensembles: A variable-barrier model for the analysis of equilibrium unfolding experiments
    • Muñoz, V.; Sanchez-Ruiz, J. M. Exploring protein folding ensembles: A variable-barrier model for the analysis of equilibrium unfolding experiments Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 17646-17651
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 17646-17651
    • Muñoz, V.1    Sanchez-Ruiz, J.M.2
  • 25
    • 3242677702 scopus 로고    scopus 로고
    • A simple thermodynamic test to discriminate between two-state and downhill folding
    • Oliva, F. Y.; Muñoz, V. A simple thermodynamic test to discriminate between two-state and downhill folding J. Am. Chem. Soc. 2004, 126, 8596-8597
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8596-8597
    • Oliva, F.Y.1    Muñoz, V.2
  • 26
    • 79953762890 scopus 로고    scopus 로고
    • Probing free-energy surfaces with differential scanning calorimetry
    • Sanchez-Ruiz, J. M. Probing free-energy surfaces with differential scanning calorimetry Annu. Rev. Phys. Chem. 2011, 62, 231-255
    • (2011) Annu. Rev. Phys. Chem. , vol.62 , pp. 231-255
    • Sanchez-Ruiz, J.M.1
  • 27
    • 0036363969 scopus 로고    scopus 로고
    • The red-edge effects: 30 years of exploration
    • Demchenko, A. P. The red-edge effects: 30 years of exploration Luminescence 2002, 17, 19-42
    • (2002) Luminescence , vol.17 , pp. 19-42
    • Demchenko, A.P.1
  • 28
    • 27744550019 scopus 로고    scopus 로고
    • Novel insights into protein structure and dynamics utilizing the red edge excitation shift approach
    • Geddes, C. D. Lakowicz, J. R. Springer, New York
    • Raghuraman, H.; Kelkar, D. A.; Chattopadhyay, A. Novel insights into protein structure and dynamics utilizing the red edge excitation shift approach. In Reviews in Fluorescence; Geddes, C. D.; Lakowicz, J. R., Eds.; Springer, New York, 2005; pp 199-222.
    • (2005) Reviews in Fluorescence , pp. 199-222
    • Raghuraman, H.1    Kelkar, D.A.2    Chattopadhyay, A.3
  • 29
    • 79956087414 scopus 로고    scopus 로고
    • Organization and dynamics of membrane probes and proteins utilizing the red edge excitation shift
    • Haldar, S.; Chaudhuri, A.; Chattopadhyay, A. Organization and dynamics of membrane probes and proteins utilizing the red edge excitation shift J. Phys. Chem. B 2011, 115, 5693-5706
    • (2011) J. Phys. Chem. B , vol.115 , pp. 5693-5706
    • Haldar, S.1    Chaudhuri, A.2    Chattopadhyay, A.3
  • 30
    • 0142210135 scopus 로고    scopus 로고
    • Organization and dynamics of tryptophan residues in erythroid spectrin: Novel structural features of denatured spectrin revealed by the wavelength-selective fluorescence approach
    • Chattopadhyay, A.; Rawat, S. S.; Kelkar, D. A.; Ray, S.; Chakrabarti, A. Organization and dynamics of tryptophan residues in erythroid spectrin: Novel structural features of denatured spectrin revealed by the wavelength-selective fluorescence approach Protein Sci. 2003, 12, 2389-2403
    • (2003) Protein Sci. , vol.12 , pp. 2389-2403
    • Chattopadhyay, A.1    Rawat, S.S.2    Kelkar, D.A.3    Ray, S.4    Chakrabarti, A.5
  • 31
    • 77956178699 scopus 로고    scopus 로고
    • Exploring tryptophan dynamics in acid-induced molten-globule state of bovine α-lactalbumin: A wavelength-selective fluorescence approach
    • Kelkar, D. A.; Chaudhuri, A.; Haldar, S.; Chattopadhyay, A. Exploring tryptophan dynamics in acid-induced molten-globule state of bovine α-lactalbumin: A wavelength-selective fluorescence approach Eur. Biophys. J. 2010, 39, 1453-1463
    • (2010) Eur. Biophys. J. , vol.39 , pp. 1453-1463
    • Kelkar, D.A.1    Chaudhuri, A.2    Haldar, S.3    Chattopadhyay, A.4
  • 32
    • 0015242342 scopus 로고
    • Effect of solvent upon the fluorescence decay of indole
    • De Lauder, W. B.; Wahl, P. H. Effect of solvent upon the fluorescence decay of indole Biochim. Biophys. Acta 1971, 243, 153-163
    • (1971) Biochim. Biophys. Acta , vol.243 , pp. 153-163
    • De Lauder, W.B.1    Wahl, P.H.2
  • 34
    • 0033554852 scopus 로고    scopus 로고
    • Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques
    • Wilkins, D. K.; Grimshaw, S. B.; Receveur, V.; Dobson, C. M.; Jones, J. A.; Smith, L. J. Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques Biochemistry 1999, 38, 16424-16431
    • (1999) Biochemistry , vol.38 , pp. 16424-16431
    • Wilkins, D.K.1    Grimshaw, S.B.2    Receveur, V.3    Dobson, C.M.4    Jones, J.A.5    Smith, L.J.6
  • 35
    • 0031019791 scopus 로고    scopus 로고
    • Molten globule of human a-lactalbumin: Hydration, density and compressibility of the interior
    • Kharakoz, D. P.; Bychkova, V. E. Molten globule of human a-lactalbumin: hydration, density and compressibility of the interior Biochemistry 1997, 36, 1882-1890
    • (1997) Biochemistry , vol.36 , pp. 1882-1890
    • Kharakoz, D.P.1    Bychkova, V.E.2
  • 36
    • 44649133131 scopus 로고    scopus 로고
    • Extrinsic fluorescent dyes as tools for protein characterization
    • Hawe, A.; Sutter, M.; Jiskoot, W. Extrinsic fluorescent dyes as tools for protein characterization Pharm. Res. 2008, 25, 1487-1499
    • (2008) Pharm. Res. , vol.25 , pp. 1487-1499
    • Hawe, A.1    Sutter, M.2    Jiskoot, W.3
  • 38
    • 77957265050 scopus 로고    scopus 로고
    • Rapid collapse into a molten globule is followed by simple two-state kinetics in the folding of lysozyme from bacteriophage ?
    • Paolo, A. D.; Balbeur, D.; Pauw, E. D.; Redfield, C.; Matagne, A. Rapid collapse into a molten globule is followed by simple two-state kinetics in the folding of lysozyme from bacteriophage ? Biochemistry 2010, 49, 8646-8657
    • (2010) Biochemistry , vol.49 , pp. 8646-8657
    • Paolo, A.D.1    Balbeur, D.2    Pauw, E.D.3    Redfield, C.4    Matagne, A.5
  • 41
    • 79961148664 scopus 로고    scopus 로고
    • The native ensemble and folding of a protein molten-globule: Functional consequence of downhill folding
    • Naganathan, A. N.; Orozco, M. The native ensemble and folding of a protein molten-globule: Functional consequence of downhill folding J. Am. Chem. Soc. 2011, 133, 12154-12161
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 12154-12161
    • Naganathan, A.N.1    Orozco, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.