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Volumn 260, Issue 2, 1999, Pages 559-567

Folding stability of the kinetoplastid membrane protein-11 (KMP-11) from Leishmania infantum

Author keywords

Circular dichroism spectroscopy; Protein folding; Protein stability; Protein structure

Indexed keywords

MEMBRANE PROTEIN; PROTOZOAL PROTEIN;

EID: 0033106288     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00217.x     Document Type: Article
Times cited : (18)

References (40)
  • 1
    • 0028854812 scopus 로고
    • Isolation and structural characterization of the Leishmania donovani kinetoplastid membrane protein-11, a major immunoreactive membrane glycoprotein
    • Jardim, A., Funk, V., Caprioli, R.M. & Olafson, R.W. (1995) Isolation and structural characterization of the Leishmania donovani kinetoplastid membrane protein-11, a major immunoreactive membrane glycoprotein. Biochem. J. 305, 307-313.
    • (1995) Biochem. J. , vol.305 , pp. 307-313
    • Jardim, A.1    Funk, V.2    Caprioli, R.M.3    Olafson, R.W.4
  • 2
    • 0028874164 scopus 로고
    • Cloning and structure-function analysis of the Leishmania donovani kinetoplastid membrane protein-11
    • Jardim, A., Hanson, S., Ullman, B., McCubbin, W.D., Kay, C.M. & Olafson, R.W. (1995) Cloning and structure-function analysis of the Leishmania donovani kinetoplastid membrane protein-11. Biochem. J. 305, 315-320.
    • (1995) Biochem. J. , vol.305 , pp. 315-320
    • Jardim, A.1    Hanson, S.2    Ullman, B.3    McCubbin, W.D.4    Kay, C.M.5    Olafson, R.W.6
  • 3
    • 0025721114 scopus 로고
    • The Leishmania donovani lipophosphoglycan T lymphocytereactive component is a tightly associated protein complex
    • Jardim, A., Tolson, D.L., Turco, S.J., Pearson, T.W. & Olafson, R.W. (1991) The Leishmania donovani lipophosphoglycan T lymphocytereactive component is a tightly associated protein complex. J. Immunol. 147, 3538-3544.
    • (1991) J. Immunol. , vol.147 , pp. 3538-3544
    • Jardim, A.1    Tolson, D.L.2    Turco, S.J.3    Pearson, T.W.4    Olafson, R.W.5
  • 4
    • 0031001121 scopus 로고    scopus 로고
    • Cloning of genes and expression and antigenicity analysis of the Leishmania infantum KMP-11 protein
    • Berberich, C., Requena, J.M. & Alonso, C. (1997) Cloning of genes and expression and antigenicity analysis of the Leishmania infantum KMP-11 protein. Exp. Parasitol. 85, 105-108.
    • (1997) Exp. Parasitol. , vol.85 , pp. 105-108
    • Berberich, C.1    Requena, J.M.2    Alonso, C.3
  • 5
    • 0025273910 scopus 로고
    • The leishmanial lipophosphoglycan: A multifunctional molecule
    • Turco, S.J. (1990) The leishmanial lipophosphoglycan: a multifunctional molecule. Exp. Parasitol. 70, 241-245.
    • (1990) Exp. Parasitol. , vol.70 , pp. 241-245
    • Turco, S.J.1
  • 6
    • 0026746610 scopus 로고
    • The lipophosphoglycan of Leishmania parasites
    • Turco, S.J. & Descoteaux, A. (1992) The lipophosphoglycan of Leishmania parasites. Annu. Rev. Microbiol. 46, 65-94.
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 65-94
    • Turco, S.J.1    Descoteaux, A.2
  • 7
    • 0023664625 scopus 로고
    • Structure of the lipid moiety of the Leishmania donovani lipphosphoglycan
    • Orlandi, P.A. & Turco, S.J. (1987) Structure of the lipid moiety of the Leishmania donovani lipphosphoglycan. J. Biol. Chem. 262, 10384-10391.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10384-10391
    • Orlandi, P.A.1    Turco, S.J.2
  • 8
    • 0024588893 scopus 로고
    • A family of glycoinositol phospholipids from Leishmania major. Isolation, characterization, and antigenicity
    • McConville, M.J. & Bacic, A. (1989) A family of glycoinositol phospholipids from Leishmania major. Isolation, characterization, and antigenicity. J. Biol. Chem. 264, 757-766.
    • (1989) J. Biol. Chem. , vol.264 , pp. 757-766
    • McConville, M.J.1    Bacic, A.2
  • 9
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S.C. & von Hippel, P.H. (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem. 182, 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 10
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang, J.T., Chuen-Shang, C.W. & Martinez, H.M. (1986) Calculation of protein conformation from circular dichroism. Methods Enzymol. 130, 208-269.
    • (1986) Methods Enzymol. , vol.130 , pp. 208-269
    • Yang, J.T.1    Chuen-Shang, C.W.2    Martinez, H.M.3
  • 11
    • 0016169865 scopus 로고
    • Determination of the helix and beta form of proteins in aqueous solution by circular dichroism
    • Chen, Y., H., Yang, J.T. & Chau, K.H. (1974) Determination of the helix and beta form of proteins in aqueous solution by circular dichroism. Biochemistry 13, 3350-3359.
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.H.1    Yang, J.T.2    Chau, K.H.3
  • 13
    • 0026496713 scopus 로고
    • Calcium-linked self-association of human complement C1s
    • Rivas, G., Ingham, K.C. & Minton, A.P. (1992) Calcium-linked self-association of human complement C1s. Biochemistry 31, 11707-11712.
    • (1992) Biochemistry , vol.31 , pp. 11707-11712
    • Rivas, G.1    Ingham, K.C.2    Minton, A.P.3
  • 15
    • 0026115704 scopus 로고
    • A strategy for efficient characterization of macromolecular heteroassociations via measurement of sedimentation equilibrium
    • Hsu, C.S. & Minton, A.P. (1991) A strategy for efficient characterization of macromolecular heteroassociations via measurement of sedimentation equilibrium. J. Mol. Recogn. 4, 93-104.
    • (1991) J. Mol. Recogn. , vol.4 , pp. 93-104
    • Hsu, C.S.1    Minton, A.P.2
  • 16
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • (Harding, S.E., Horton, H.C. & Rowe, A.J., eds.). Royal Society of Chemistry, London
    • Laue, T.M., Shah, B.D., Ridgeway, T.M. & Pelletier, S.L. (1993). Computer-aided interpretation of analytical sedimentation data for proteins. In Analytical Ultracentrifugation in Biochemistry and Polymer Science. (Harding, S.E., Horton, H.C. & Rowe, A.J., eds.), pp. 90-125. Royal Society of Chemistry, London.
    • (1993) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 19
    • 0025330550 scopus 로고
    • New B-cell epitopes in the Plasmodium falciparum malaria circumsporozoite protein
    • Stüber, D., Bannwarth, W., Pink, J.R.L., Meloen, R.H. & Matile, H. (1990) New B-cell epitopes in the Plasmodium falciparum malaria circumsporozoite protein. Eur. J. Immunol. 20, 819-824.
    • (1990) Eur. J. Immunol. , vol.20 , pp. 819-824
    • Stüber, D.1    Bannwarth, W.2    Pink, J.R.L.3    Meloen, R.H.4    Matile, H.5
  • 20
    • 0025951267 scopus 로고
    • Preparation of clinical grade proteins produced by recombinant DNA technologies
    • Takacs, B.J. & Girard, M-F. (1991) Preparation of clinical grade proteins produced by recombinant DNA technologies, J. Immunol. Meth 143, 231-240.
    • (1991) J. Immunol. Meth. , vol.143 , pp. 231-240
    • Takacs, B.J.1    Girard, M.-F.2
  • 21
    • 0015870378 scopus 로고
    • Circular dichroism and optical rotatory dispersion of proteins and polypeptides
    • Adler, J.T., Greenfield, N.J. & Fasman, G.D. (1973) Circular dichroism and optical rotatory dispersion of proteins and polypeptides. Methods Enzymol. 27, 675-735.
    • (1973) Methods Enzymol. , vol.27 , pp. 675-735
    • Adler, J.T.1    Greenfield, N.J.2    Fasman, G.D.3
  • 22
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • Chou, P.Y. & Fasman, G.D. (1974) Prediction of protein conformation. Biochemistry 13, 222-245.
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 23
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N. & Fasman, G.D. (1969) Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8, 4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 24
    • 0023122030 scopus 로고
    • Tests of the helix dipole model for stabilization of alphahelices
    • Shoemaker, K.R., Kim, P.S., York, E.J., Stewart, J.M. & Baldwin, R.L. (1987) Tests of the helix dipole model for stabilization of alphahelices. Nature 326, 563-567.
    • (1987) Nature , vol.326 , pp. 563-567
    • Shoemaker, K.R.1    Kim, P.S.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 25
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C.N. (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Emzymol. 131, 266-279.
    • (1986) Methods Emzymol. , vol.131 , pp. 266-279
    • Pace, C.N.1
  • 26
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • Santoro, M.M. & Bolen, D.W. (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27, 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 27
    • 0015950692 scopus 로고
    • A molecular theory of lipid-protein interactions in the plasma lipoproteins
    • Segrest, J.P., Jackson, R.L., Morrisett, J.D. & Gotto, A.M. Jr (1974) A molecular theory of lipid-protein interactions in the plasma lipoproteins. FEBS Lett. 38, 247-253.
    • (1974) FEBS Lett. , vol.38 , pp. 247-253
    • Segrest, J.P.1    Jackson, R.L.2    Morrisett, J.D.3    Gotto A.M., Jr.4
  • 28
    • 0025860481 scopus 로고
    • Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E
    • Wilson, C., Wardell, M.R., Weisgraber, K.H., Mahley, R.W. & Agard, D.A. (1991) Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E. Science 252, 1817-1822.
    • (1991) Science , vol.252 , pp. 1817-1822
    • Wilson, C.1    Wardell, M.R.2    Weisgraber, K.H.3    Mahley, R.W.4    Agard, D.A.5
  • 29
    • 0027391142 scopus 로고
    • Conformational, thermodynamic, and stability properties of Manduca sexta apolipophorin III
    • Ryan, R.O., Oikawa, K. & Kay, C.M. (1993) Conformational, thermodynamic, and stability properties of Manduca sexta apolipophorin III. J. Biol. Chem. 268, 1525-1530.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1525-1530
    • Ryan, R.O.1    Oikawa, K.2    Kay, C.M.3
  • 30
    • 0016609354 scopus 로고
    • The molecular behavior of apoA-I in human high density lipoproteins
    • Gwynne, J., Brewer, H.B. Jr & Edelhoch, H. (1975b) The molecular behavior of apoA-I in human high density lipoproteins. J. Biol. Chem. 250, 2269-2274.
    • (1975) J. Biol. Chem. , vol.250 , pp. 2269-2274
    • Gwynne, J.1    Brewer H.B., Jr.2    Edelhoch, H.3
  • 31
    • 0015887968 scopus 로고
    • Ionization behavior of glutamic acid 35 and a tyrosyl residue of hen egg-white lysozyme
    • Nakae, Y., Ikeda, K. & Hamaguchi, K. (1973) Ionization behavior of glutamic acid 35 and a tyrosyl residue of hen egg-white lysozyme. J. Biochem. (Tokyo) 73, 1249-1256.
    • (1973) J. Biochem. (Tokyo) , vol.73 , pp. 1249-1256
    • Nakae, Y.1    Ikeda, K.2    Hamaguchi, K.3
  • 32
    • 0014354873 scopus 로고
    • Fluorescence spectroscopy of proteins
    • Stryer, L. (1968) Fluorescence spectroscopy of proteins. Science 162, 526-533.
    • (1968) Science , vol.162 , pp. 526-533
    • Stryer, L.1
  • 33
    • 0014342841 scopus 로고
    • Quantitative estimation of protein binding site polarity. Fluorescence of N-arylaminonaphthalenesulfonates
    • Turner, D.C. & Brand, L. (1968) Quantitative estimation of protein binding site polarity. Fluorescence of N-arylaminonaphthalenesulfonates. Biochemistry 7, 3381-3390.
    • (1968) Biochemistry , vol.7 , pp. 3381-3390
    • Turner, D.C.1    Brand, L.2
  • 35
    • 0025216077 scopus 로고
    • An early immunoreactive folding intermediate of the tryptopban synthease beta 2 subunit is a 'molten globule'
    • Goldberg, M.E., Semisotnov, G.V., Friguet, B., Kuwajima, K., Ptitsyn, O.B. & Sugai, S. (1990) An early immunoreactive folding intermediate of the tryptopban synthease beta 2 subunit is a 'molten globule'. FEBS Lett. 263, 51-56.
    • (1990) FEBS Lett. , vol.263 , pp. 51-56
    • Goldberg, M.E.1    Semisotnov, G.V.2    Friguet, B.3    Kuwajima, K.4    Ptitsyn, O.B.5    Sugai, S.6
  • 36
    • 0025938928 scopus 로고
    • Proposed molten globule intermediates in fd phage penetration and assembly
    • Dunker, A.K., Ensign, L.D., Arnold, G.E. & Roberts, L.M. (1991) Proposed molten globule intermediates in fd phage penetration and assembly. FEBS Lett. 292, 275-278.
    • (1991) FEBS Lett. , vol.292 , pp. 275-278
    • Dunker, A.K.1    Ensign, L.D.2    Arnold, G.E.3    Roberts, L.M.4
  • 37
    • 0030592481 scopus 로고    scopus 로고
    • Molecular characterization of the kinetoplastid membrane protein-11 from African trypanosomes
    • Stebeck, C.E., Baron, G.S., Beecroft, R.P. & Pearson, T.W. (1996) Molecular characterization of the kinetoplastid membrane protein-11 from African trypanosomes. Mol. Biochem. Parasitol. 81, 81-88.
    • (1996) Mol. Biochem. Parasitol. , vol.81 , pp. 81-88
    • Stebeck, C.E.1    Baron, G.S.2    Beecroft, R.P.3    Pearson, T.W.4
  • 38
    • 0021835796 scopus 로고
    • Structural properties and lipid binding of human apolipoprotein A-IV
    • Weinberg, R.D. & Spector, M.S. (1985b) Structural properties and lipid binding of human apolipoprotein A-IV. J. Biol. Chem. 260, 4914-4921.
    • (1985) J. Biol. Chem. , vol.260 , pp. 4914-4921
    • Weinberg, R.D.1    Spector, M.S.2
  • 39
    • 0020119906 scopus 로고
    • A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A
    • Bierzynski, A., Kim, P.S. & Baldwin, R.L. (1982) A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A. Proc. Natl Acad. Sci. USA 79, 2470-2474.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 2470-2474
    • Bierzynski, A.1    Kim, P.S.2    Baldwin, R.L.3


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