메뉴 건너뛰기




Volumn 1818, Issue 4, 2012, Pages 1049-1054

Thermodynamic stability of bacteriorhodopsin mutants measured relative to the bacterioopsin unfolded state

Author keywords

Folding kinetics; Membrane protein; Protein folding; SDS

Indexed keywords

BACTERIAL PROTEIN; BACTERIOPSIN; BACTERIORHODOPSIN; MUTANT PROTEIN; UNCLASSIFIED DRUG;

EID: 84857650575     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.08.019     Document Type: Article
Times cited : (16)

References (29)
  • 1
    • 0025129186 scopus 로고
    • Thermal stability of membrane-reconstituted yeast cytochrome c oxidase
    • P.E. Morin, D. Diggs, and E. Freire Thermal stability of membrane-reconstituted yeast cytochrome c oxidase Biochemistry 29 1990 781 788
    • (1990) Biochemistry , vol.29 , pp. 781-788
    • Morin, P.E.1    Diggs, D.2    Freire, E.3
  • 3
    • 0023768321 scopus 로고
    • Structural stability of the erythrocyte anion transporter, band 3, in different lipid environments. A differential scanning calorimetric study
    • L.R. Maneri, and P.S. Low Structural stability of the erythrocyte anion transporter, band 3, in different lipid environments. A differential scanning calorimetric study J. Biol. Chem. 263 1988 16170 16178
    • (1988) J. Biol. Chem. , vol.263 , pp. 16170-16178
    • Maneri, L.R.1    Low, P.S.2
  • 4
    • 0031437768 scopus 로고    scopus 로고
    • Reduction of membrane protein hydrophobicity by site-directed mutagenesis: Introduction of multiple polar residues in helix D of bacteriorhodopsin
    • G.Q. Chen, and E. Gouaux Reduction of membrane protein hydrophobicity by site-directed mutagenesis: introduction of multiple polar residues in helix D of bacteriorhodopsin Protein Eng. 10 1997 1061 1066
    • (1997) Protein Eng. , vol.10 , pp. 1061-1066
    • Chen, G.Q.1    Gouaux, E.2
  • 5
    • 0026686623 scopus 로고
    • Thermodynamic measurements of the contributions of helix-connecting loops and of retinal to the stability of bacteriorhodopsin
    • T.W. Kahn, J.M. Sturtevant, and D.M. Engelman Thermodynamic measurements of the contributions of helix-connecting loops and of retinal to the stability of bacteriorhodopsin Biochemistry 31 1992 8829 8839
    • (1992) Biochemistry , vol.31 , pp. 8829-8839
    • Kahn, T.W.1    Sturtevant, J.M.2    Engelman, D.M.3
  • 6
    • 0029112313 scopus 로고
    • Forces and factors that contribute to the structural stability of membrane proteins
    • T. Haltia, and E. Freire Forces and factors that contribute to the structural stability of membrane proteins Biochim. Biophys. Acta 1241 1995 295 322
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 295-322
    • Haltia, T.1    Freire, E.2
  • 7
    • 77349083921 scopus 로고    scopus 로고
    • Reversible unfolding of a thermophilic membrane protein in phospholipid/detergent mixed micelles
    • E.A. Roman, J.M. Argüello, and F.L. González Flecha Reversible unfolding of a thermophilic membrane protein in phospholipid/ detergent mixed micelles J. Mol. Biol. 397 2010 550 559
    • (2010) J. Mol. Biol. , vol.397 , pp. 550-559
    • Roman, E.A.1    Argüello, J.M.2    González Flecha, F.L.3
  • 9
    • 0031010621 scopus 로고    scopus 로고
    • A method for assessing the stability of a membrane protein
    • F.W. Lau, and J.U. Bowie A method for assessing the stability of a membrane protein Biochemistry 36 1997 5884 5892
    • (1997) Biochemistry , vol.36 , pp. 5884-5892
    • Lau, F.W.1    Bowie, J.U.2
  • 10
    • 33845428343 scopus 로고    scopus 로고
    • An unfolding story of helical transmembrane proteins
    • R. Renthal An unfolding story of helical transmembrane proteins Biochemistry 45 2006 14559 14566
    • (2006) Biochemistry , vol.45 , pp. 14559-14566
    • Renthal, R.1
  • 11
    • 0019887931 scopus 로고
    • Refolding of an integral membrane protein. Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments
    • K.S. Huang, H. Bayley, M.J. Liao, E. London, and H.G. Khorana Refolding of an integral membrane protein. Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments J. Biol. Chem. 256 1981 3802 3809
    • (1981) J. Biol. Chem. , vol.256 , pp. 3802-3809
    • Huang, K.S.1    Bayley, H.2    Liao, M.J.3    London, E.4    Khorana, H.G.5
  • 12
    • 0020429978 scopus 로고
    • Factors determining the reconstructive denaturation of proteins in sodium dodecyl sulfate solutions. Further circular dichroism studies on structural reorganization of seven proteins
    • B. Jirgensons Factors determining the reconstructive denaturation of proteins in sodium dodecyl sulfate solutions. Further circular dichroism studies on structural reorganization of seven proteins J. Protein Chem. 1 1982 71 84
    • (1982) J. Protein Chem. , vol.1 , pp. 71-84
    • Jirgensons, B.1
  • 13
    • 0014964805 scopus 로고
    • Effect of sodium dodecyl sulfate on circular dichroism of some nonhelical proteins
    • B. Jirgensons, and S. Capetillo Effect of sodium dodecyl sulfate on circular dichroism of some nonhelical proteins Biochim. Biophys. Acta 214 1970 1 5
    • (1970) Biochim. Biophys. Acta , vol.214 , pp. 1-5
    • Jirgensons, B.1    Capetillo, S.2
  • 14
    • 0025828328 scopus 로고
    • Interaction of apocytochrome c and derived polypeptide fragments with sodium dodecyl sulfate micelles monitored by photochemically induced dynamic nuclear polarization 1H NMR and fluorescence spectroscopy
    • M.M. Snel, R. Kaptein, and B. de Kruijff Interaction of apocytochrome c and derived polypeptide fragments with sodium dodecyl sulfate micelles monitored by photochemically induced dynamic nuclear polarization 1H NMR and fluorescence spectroscopy Biochemistry 30 1991 3387 3395
    • (1991) Biochemistry , vol.30 , pp. 3387-3395
    • Snel, M.M.1    Kaptein, R.2    De Kruijff, B.3
  • 15
    • 0020490831 scopus 로고
    • Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures
    • E. London, and H.G. Khorana Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures J. Biol. Chem. 257 1982 7003 7011
    • (1982) J. Biol. Chem. , vol.257 , pp. 7003-7011
    • London, E.1    Khorana, H.G.2
  • 16
    • 0032502747 scopus 로고    scopus 로고
    • Refolding of bacteriorhodopsin from expressed polypeptide fragments
    • T. Marti Refolding of bacteriorhodopsin from expressed polypeptide fragments J. Biol. Chem. 273 1998 9312 9322
    • (1998) J. Biol. Chem. , vol.273 , pp. 9312-9322
    • Marti, T.1
  • 17
    • 37649004552 scopus 로고    scopus 로고
    • Combined kinetic and thermodynamic analysis of alpha-helical membrane protein unfolding
    • P. Curnow, and P.J. Booth Combined kinetic and thermodynamic analysis of alpha-helical membrane protein unfolding Proc. Natl. Acad. Sci. U. S. A. 104 2007 18970 18975
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 18970-18975
    • Curnow, P.1    Booth, P.J.2
  • 18
    • 58849112736 scopus 로고    scopus 로고
    • The transition state for integral membrane protein folding
    • P. Curnow, and P.J. Booth The transition state for integral membrane protein folding Proc. Natl. Acad. Sci. U. S. A. 106 2009 773 778
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 773-778
    • Curnow, P.1    Booth, P.J.2
  • 22
    • 0742288411 scopus 로고    scopus 로고
    • The evolution of transmembrane helix kinks and the structural diversity of G protein-coupled receptors
    • S. Yohannan, S. Faham, D. Yang, J.P. Whitelegge, and J.U. Bowie The evolution of transmembrane helix kinks and the structural diversity of G protein-coupled receptors Proc. Natl. Acad. Sci. U. S. A. 101 2004 959 963
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 959-963
    • Yohannan, S.1    Faham, S.2    Yang, D.3    Whitelegge, J.P.4    Bowie, J.U.5
  • 24
    • 46249089993 scopus 로고    scopus 로고
    • Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins
    • N.H. Joh, A. Min, S. Faham, J.P. Whitelegge, D. Yang, and V.L. Woods Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins Nature 453 2008 1266 1270
    • (2008) Nature , vol.453 , pp. 1266-1270
    • Joh, N.H.1    Min, A.2    Faham, S.3    Whitelegge, J.P.4    Yang, D.5    Woods, V.L.6
  • 25
    • 68249144241 scopus 로고    scopus 로고
    • Similar energetic contributions of packing in the core of membrane and water-soluble proteins
    • N.H. Joh, A. Oberai, D. Yang, J.P. Whitelegge, and J.U. Bowie Similar energetic contributions of packing in the core of membrane and water-soluble proteins J. Am. Chem. Soc. 131 2009 10846 10847
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 10846-10847
    • Joh, N.H.1    Oberai, A.2    Yang, D.3    Whitelegge, J.P.4    Bowie, J.U.5
  • 26
    • 0001041988 scopus 로고    scopus 로고
    • Probing the folding and unfolding of wild-type and mutant forms of bacteriorhodopsin in micellar solutions: Evaluation of reversible unfolding conditions
    • G.Q. Chen, and E. Gouaux Probing the folding and unfolding of wild-type and mutant forms of bacteriorhodopsin in micellar solutions: evaluation of reversible unfolding conditions Biochemistry 38 1999 15380 15387
    • (1999) Biochemistry , vol.38 , pp. 15380-15387
    • Chen, G.Q.1    Gouaux, E.2
  • 27
    • 0023099215 scopus 로고
    • Efficient transfection of the archaebacterium Halobacterium halobium
    • S.W. Cline, and W.F. Doolittle Efficient transfection of the archaebacterium Halobacterium halobium J. Bacteriol. 169 1987 1341 1344
    • (1987) J. Bacteriol. , vol.169 , pp. 1341-1344
    • Cline, S.W.1    Doolittle, W.F.2
  • 28
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
    • D. Oesterhelt, and W. Stoeckenius Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane Methods Enzymol. 31 1974 667 678
    • (1974) Methods Enzymol. , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 29
    • 0001448722 scopus 로고
    • Mechanism of retinal Schiff base formation and hydrolysis in relation to visual pigment photolysis and regeneration: Resonance Raman spectroscopy of a tetrahedral carbinolamine intermediate and oxygen-18 labeling of retinal at the metarhodopsin stage in photoreceptor membranes
    • A. Cooper, S.F. Dixon, M.A. Nutley, and J.L. Robb Mechanism of retinal Schiff base formation and hydrolysis in relation to visual pigment photolysis and regeneration: resonance Raman spectroscopy of a tetrahedral carbinolamine intermediate and oxygen-18 labeling of retinal at the metarhodopsin stage in photoreceptor membranes J. Am. Chem. Soc. 109 1987 7254 7263
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 7254-7263
    • Cooper, A.1    Dixon, S.F.2    Nutley, M.A.3    Robb, J.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.