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Volumn 124, Issue 2, 2006, Pages 115-124

Effect of ionic strength on the organization and dynamics of membrane-bound melittin

Author keywords

Acrylamide quenching; Ionic strength; Lipid protein interaction; Melittin organization; Red edge excitation shift; Tryptophan fluorescence

Indexed keywords

ACRYLAMIDE; ION; MELITTIN; MEMBRANE PROTEIN; PEPTIDE; PROTEIN; SOLVENT; TRYPTOPHAN;

EID: 33750171887     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2006.06.011     Document Type: Article
Times cited : (25)

References (60)
  • 1
    • 0015527253 scopus 로고
    • Bee and wasp venoms
    • Habermann E. Bee and wasp venoms. Science 177 (1972) 314-322
    • (1972) Science , vol.177 , pp. 314-322
    • Habermann, E.1
  • 2
    • 0025217893 scopus 로고
    • The actions of melittin on membranes
    • Dempsey C.E. The actions of melittin on membranes. Biochim. Biophys. Acta 1031 (1990) 143-161
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 143-161
    • Dempsey, C.E.1
  • 3
    • 0028339191 scopus 로고
    • Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: facets of their conformational features, structure-function correlation and membrane-perturbing abilities
    • Saberwal G., and Nagaraj R. Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: facets of their conformational features, structure-function correlation and membrane-perturbing abilities. Biochim. Biophys. Acta 1197 (1994) 109-131
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 109-131
    • Saberwal, G.1    Nagaraj, R.2
  • 4
    • 0028788193 scopus 로고
    • Molecular recognition between membrane-spanning polypeptides
    • Shai Y. Molecular recognition between membrane-spanning polypeptides. Trends Biochem. Sci. 20 (1995) 460-464
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 460-464
    • Shai, Y.1
  • 5
    • 0030981655 scopus 로고    scopus 로고
    • Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin
    • Bechinger B. Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin. J. Membr. Biol. 156 (1997) 197-211
    • (1997) J. Membr. Biol. , vol.156 , pp. 197-211
    • Bechinger, B.1
  • 6
    • 0020473234 scopus 로고
    • Conformation and aggregation of melittin: dependence on pH and concentration
    • Bello J., Bello H.R., and Granados E. Conformation and aggregation of melittin: dependence on pH and concentration. Biochemistry 21 (1982) 461-465
    • (1982) Biochemistry , vol.21 , pp. 461-465
    • Bello, J.1    Bello, H.R.2    Granados, E.3
  • 7
    • 0028598299 scopus 로고
    • Analysis of circular dichroism spectra of oriented protein-lipid complexes: toward a general application
    • De Jongh H.H.J., Goormaghtigh E., and Killian J.A. Analysis of circular dichroism spectra of oriented protein-lipid complexes: toward a general application. Biochemistry 33 (1994) 14521-14528
    • (1994) Biochemistry , vol.33 , pp. 14521-14528
    • De Jongh, H.H.J.1    Goormaghtigh, E.2    Killian, J.A.3
  • 9
    • 0030704248 scopus 로고    scopus 로고
    • Modulation of tryptophan environment in membrane-bound melittin by negatively charged phospholipids: implications in membrane organization and function
    • Ghosh A.K., Rukmini R., and Chattopadhyay A. Modulation of tryptophan environment in membrane-bound melittin by negatively charged phospholipids: implications in membrane organization and function. Biochemistry 36 (1997) 14291-14305
    • (1997) Biochemistry , vol.36 , pp. 14291-14305
    • Ghosh, A.K.1    Rukmini, R.2    Chattopadhyay, A.3
  • 10
    • 15244358803 scopus 로고    scopus 로고
    • Interaction of melittin with membrane cholesterol: a fluorescence approach
    • Raghuraman H., and Chattopadhyay A. Interaction of melittin with membrane cholesterol: a fluorescence approach. Biophys. J. 87 (2004) 2419-2432
    • (2004) Biophys. J. , vol.87 , pp. 2419-2432
    • Raghuraman, H.1    Chattopadhyay, A.2
  • 11
    • 4644333025 scopus 로고    scopus 로고
    • Influence of lipid chain unsaturation on membrane-bound melittin: a fluorescence approach
    • Raghuraman H., and Chattopadhyay A. Influence of lipid chain unsaturation on membrane-bound melittin: a fluorescence approach. Biochim. Biophys. Acta 1665 (2004) 29-39
    • (2004) Biochim. Biophys. Acta , vol.1665 , pp. 29-39
    • Raghuraman, H.1    Chattopadhyay, A.2
  • 12
    • 0345376179 scopus 로고    scopus 로고
    • Organization and dynamics of melittin in environments of graded hydration: a fluorescence approach
    • Raghuraman H., and Chattopadhyay A. Organization and dynamics of melittin in environments of graded hydration: a fluorescence approach. Langmuir 19 (2003) 10332-10341
    • (2003) Langmuir , vol.19 , pp. 10332-10341
    • Raghuraman, H.1    Chattopadhyay, A.2
  • 13
    • 4143110587 scopus 로고    scopus 로고
    • Effect of micellar charge on the conformation and dynamics of melittin
    • Raghuraman H., and Chattopadhyay A. Effect of micellar charge on the conformation and dynamics of melittin. Eur. Biophys. J. 33 (2004) 611-622
    • (2004) Eur. Biophys. J. , vol.33 , pp. 611-622
    • Raghuraman, H.1    Chattopadhyay, A.2
  • 15
    • 0013358476 scopus 로고
    • Secondary structures of proteins and peptides in amphiphilic environment
    • Kaiser E.T., and Kezdy F.J. Secondary structures of proteins and peptides in amphiphilic environment. Proc. Natl. Acad. Sci. U. S. A. 80 (1983) 1137-1143
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 1137-1143
    • Kaiser, E.T.1    Kezdy, F.J.2
  • 16
    • 0028166610 scopus 로고
    • Alpha-helical assembly of biologically active peptides and designed helix bundle protein
    • Morii H.S., Honda S., Ohashi S., and Uedaira H. Alpha-helical assembly of biologically active peptides and designed helix bundle protein. Biopolymers 34 (1994) 481-488
    • (1994) Biopolymers , vol.34 , pp. 481-488
    • Morii, H.S.1    Honda, S.2    Ohashi, S.3    Uedaira, H.4
  • 17
    • 0028823176 scopus 로고
    • The interactions of signal sequences with membranes
    • Golding C., and O' Shea P. The interactions of signal sequences with membranes. Biochem. Soc. Trans. 23 (1995) 971-976
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 971-976
    • Golding, C.1    O' Shea, P.2
  • 18
    • 0028838458 scopus 로고
    • A peptide from the heptad repeat of human immunodeficiency virus gp41 shows both membrane binding and coiled-coil formation
    • Rabenstein M., and Shin Y.K. A peptide from the heptad repeat of human immunodeficiency virus gp41 shows both membrane binding and coiled-coil formation. Biochemistry 34 (1995) 13390-13397
    • (1995) Biochemistry , vol.34 , pp. 13390-13397
    • Rabenstein, M.1    Shin, Y.K.2
  • 19
    • 0030997633 scopus 로고    scopus 로고
    • Solution structure of polypeptide from the N terminus of the HIV protein Nef
    • Barnham K.J., Monks S.A., Hinds M.G., Azad A.A., and Norton R.S. Solution structure of polypeptide from the N terminus of the HIV protein Nef. Biochemistry 36 (1997) 5970-5980
    • (1997) Biochemistry , vol.36 , pp. 5970-5980
    • Barnham, K.J.1    Monks, S.A.2    Hinds, M.G.3    Azad, A.A.4    Norton, R.S.5
  • 20
    • 0030909316 scopus 로고    scopus 로고
    • Synergism between melittin and phospholipase A2 from bee venom: apparent activation by intervesicle exchange of phospholipids
    • Cajal Y., and Jain M.K. Synergism between melittin and phospholipase A2 from bee venom: apparent activation by intervesicle exchange of phospholipids. Biochemistry 36 (1997) 3882-3893
    • (1997) Biochemistry , vol.36 , pp. 3882-3893
    • Cajal, Y.1    Jain, M.K.2
  • 21
    • 0028784395 scopus 로고
    • Stopped-flow fluorometric study of the interaction of melittin with phospholipid bilayers: importance of the physical state of the bilayer and the acyl chain length
    • Bradrick T.D., Philippetis A., and Georghiou S. Stopped-flow fluorometric study of the interaction of melittin with phospholipid bilayers: importance of the physical state of the bilayer and the acyl chain length. Biophys. J. 69 (1995) 1999-2010
    • (1995) Biophys. J. , vol.69 , pp. 1999-2010
    • Bradrick, T.D.1    Philippetis, A.2    Georghiou, S.3
  • 22
    • 0031024551 scopus 로고    scopus 로고
    • Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study
    • Oren Z., and Shai Y. Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study. Biochemistry 36 (1997) 1826-1835
    • (1997) Biochemistry , vol.36 , pp. 1826-1835
    • Oren, Z.1    Shai, Y.2
  • 23
    • 0014824452 scopus 로고
    • Modifications of amino groups and tryptophan in melittin as an aid to recognition of structure-activity relationships
    • Habermann E., and Kowallek H. Modifications of amino groups and tryptophan in melittin as an aid to recognition of structure-activity relationships. Hoppe-Seylers Z. Physiol. Chem. 351 (1970) 884-890
    • (1970) Hoppe-Seylers Z. Physiol. Chem. , vol.351 , pp. 884-890
    • Habermann, E.1    Kowallek, H.2
  • 24
    • 0025717603 scopus 로고
    • Probing the relationships between the structure and hemolytic activity of melittin with a complete set of leucine substitution analogues
    • Blondelle S.E., and Houghten R.A. Probing the relationships between the structure and hemolytic activity of melittin with a complete set of leucine substitution analogues. J. Pept. Res. 4 (1991) 12-18
    • (1991) J. Pept. Res. , vol.4 , pp. 12-18
    • Blondelle, S.E.1    Houghten, R.A.2
  • 25
    • 0025833449 scopus 로고
    • Hemolytic and antimicrobial activities of twenty-four individual omission analogues of melittin
    • Blondelle S.E., and Houghten R.A. Hemolytic and antimicrobial activities of twenty-four individual omission analogues of melittin. Biochemistry 30 (1991) 4671-4678
    • (1991) Biochemistry , vol.30 , pp. 4671-4678
    • Blondelle, S.E.1    Houghten, R.A.2
  • 26
    • 0027363792 scopus 로고
    • Restricted mobility of the sole tryptophan in membrane-bound melittin
    • Chattopadhyay A., and Rukmini R. Restricted mobility of the sole tryptophan in membrane-bound melittin. FEBS Lett. 335 (1993) 341-344
    • (1993) FEBS Lett. , vol.335 , pp. 341-344
    • Chattopadhyay, A.1    Rukmini, R.2
  • 27
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • Yau W.M., Wimley W.C., Gawrisch K., and White S.H. The preference of tryptophan for membrane interfaces. Biochemistry 37 (1998) 14713-14718
    • (1998) Biochemistry , vol.37 , pp. 14713-14718
    • Yau, W.M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4
  • 28
    • 0037881905 scopus 로고    scopus 로고
    • Interfacial anchor properties of tryptophan residues in transmembrane peptides can dominate over hydrophobic matching effects in peptide-lipid interactions
    • de Planque M.R., Bonev B.B., Demmers J.A., Greathouse D.V., Koeppe R.E., Separovic F., Watts A., and Killian J.A. Interfacial anchor properties of tryptophan residues in transmembrane peptides can dominate over hydrophobic matching effects in peptide-lipid interactions. Biochemistry 42 (2003) 5341-5348
    • (2003) Biochemistry , vol.42 , pp. 5341-5348
    • de Planque, M.R.1    Bonev, B.B.2    Demmers, J.A.3    Greathouse, D.V.4    Koeppe, R.E.5    Separovic, F.6    Watts, A.7    Killian, J.A.8
  • 29
    • 0034859096 scopus 로고    scopus 로고
    • Barrel-stave model or toroidal model ? A case study on melittin pores
    • Yang L., Harroun T.A., Weiss T.M., Ding L., and Huang H.W. Barrel-stave model or toroidal model ? A case study on melittin pores. Biophys. J. 81 (2001) 1475-1485
    • (2001) Biophys. J. , vol.81 , pp. 1475-1485
    • Yang, L.1    Harroun, T.A.2    Weiss, T.M.3    Ding, L.4    Huang, H.W.5
  • 30
    • 0028084309 scopus 로고
    • Lipid unsaturation influences melittin-induced leakage of vesicles
    • Subbarao N.K., and MacDonald R.C. Lipid unsaturation influences melittin-induced leakage of vesicles. Biochim. Biophys. Acta 1189 (1994) 101-107
    • (1994) Biochim. Biophys. Acta , vol.1189 , pp. 101-107
    • Subbarao, N.K.1    MacDonald, R.C.2
  • 31
    • 15244356065 scopus 로고    scopus 로고
    • Cholesterol inhibits the lytic activity of melittin in erythrocytes
    • Raghuraman H., and Chattopadhyay A. Cholesterol inhibits the lytic activity of melittin in erythrocytes. Chem. Phys. Lipids 134 (2005) 183-189
    • (2005) Chem. Phys. Lipids , vol.134 , pp. 183-189
    • Raghuraman, H.1    Chattopadhyay, A.2
  • 32
    • 78651157652 scopus 로고
    • Simple, specific spray for the detection of phospholipids on the thin-layer chromatograms
    • Dittmer J.C., and Lester R.L. Simple, specific spray for the detection of phospholipids on the thin-layer chromatograms. J. Lipid Res. 5 (1964) 126-127
    • (1964) J. Lipid Res. , vol.5 , pp. 126-127
    • Dittmer, J.C.1    Lester, R.L.2
  • 33
    • 0015019307 scopus 로고
    • An accurate and convenient organic phosphorus assay
    • McClare C.W.F. An accurate and convenient organic phosphorus assay. Anal. Biochem. 39 (1971) 527-530
    • (1971) Anal. Biochem. , vol.39 , pp. 527-530
    • McClare, C.W.F.1
  • 34
    • 0002848296 scopus 로고
    • Fluorescence quenching reactions: probing biological macromolecular structure
    • Dewey T.G. (Ed), Plenum Press, New York
    • Eftink M.R. Fluorescence quenching reactions: probing biological macromolecular structure. In: Dewey T.G. (Ed). Biophysical and Biochemical Aspects of Fluorescence Spectroscopy (1991), Plenum Press, New York 1-41
    • (1991) Biophysical and Biochemical Aspects of Fluorescence Spectroscopy , pp. 1-41
    • Eftink, M.R.1
  • 36
    • 0000367088 scopus 로고
    • Two-point calibration of circular dichrometer with d-10-camphorsulfonic acid
    • Chen G.C., and Yang J.T. Two-point calibration of circular dichrometer with d-10-camphorsulfonic acid. Anal. Lett. 10 (1977) 1195-1207
    • (1977) Anal. Lett. , vol.10 , pp. 1195-1207
    • Chen, G.C.1    Yang, J.T.2
  • 37
    • 0037277845 scopus 로고    scopus 로고
    • Exploring membrane organization and dynamics by the wavelength-selective fluorescence approach
    • Chattopadhyay A. Exploring membrane organization and dynamics by the wavelength-selective fluorescence approach. Chem. Phys. Lipids 122 (2003) 3-17
    • (2003) Chem. Phys. Lipids , vol.122 , pp. 3-17
    • Chattopadhyay, A.1
  • 38
    • 27744550019 scopus 로고    scopus 로고
    • Novel insights into membrane protein structure and dynamics utilizing the red edge excitation shift
    • Geddes C.D., and Lakowicz J.R. (Eds), Springer, New York
    • Raghuraman H., Kelkar D.A., and Chattopadhyay A. Novel insights into membrane protein structure and dynamics utilizing the red edge excitation shift. In: Geddes C.D., and Lakowicz J.R. (Eds). Reviews in Fluorescence 2005 vol. 2 (2005), Springer, New York 199-222
    • (2005) Reviews in Fluorescence 2005 , vol.2 , pp. 199-222
    • Raghuraman, H.1    Kelkar, D.A.2    Chattopadhyay, A.3
  • 39
    • 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 17 (2002) 19-42
    • (2002) Luminescence , vol.17 , pp. 19-42
    • Demchenko, A.P.1
  • 40
    • 0013228332 scopus 로고    scopus 로고
    • Mentré P. (Ed)
    • In: Mentré P. (Ed). Water in the Cell. Cell. Mol. Biol. vol. 47 (2001) 709-970
    • (2001) Cell. Mol. Biol. , vol.47 , pp. 709-970
  • 41
    • 1442263781 scopus 로고    scopus 로고
    • Effect of urea on the organization and dynamics of Triton X-100 micelles: a fluorescence approach
    • Raghuraman H., Pradhan S.K., and Chattopadhyay A. Effect of urea on the organization and dynamics of Triton X-100 micelles: a fluorescence approach. J. Phys. Chem., B 108 (2004) 2489-2496
    • (2004) J. Phys. Chem., B , vol.108 , pp. 2489-2496
    • Raghuraman, H.1    Pradhan, S.K.2    Chattopadhyay, A.3
  • 42
    • 11844305944 scopus 로고    scopus 로고
    • Influence of ester and ether linkage in phospholipids on the organization and dynamics of the membrane interface: a wavelength-selective fluorescence approach
    • Mukherjee S., and Chattopadhyay A. Influence of ester and ether linkage in phospholipids on the organization and dynamics of the membrane interface: a wavelength-selective fluorescence approach. Langmuir 21 (2005) 287-293
    • (2005) Langmuir , vol.21 , pp. 287-293
    • Mukherjee, S.1    Chattopadhyay, A.2
  • 43
    • 14744278408 scopus 로고    scopus 로고
    • Monitoring cholesterol organization in membranes at low concentrations utilizing the wavelength-selective fluorescence approach
    • Mukherjee S., and Chattopadhyay A. Monitoring cholesterol organization in membranes at low concentrations utilizing the wavelength-selective fluorescence approach. Chem. Phys. Lipids 134 (2005) 79-84
    • (2005) Chem. Phys. Lipids , vol.134 , pp. 79-84
    • Mukherjee, S.1    Chattopadhyay, A.2
  • 44
    • 4143084797 scopus 로고    scopus 로고
    • Monitoring gramicidin conformations in membranes: a fluorescence approach
    • Rawat S.S., Kelkar D.A., and Chattopadhyay A. Monitoring gramicidin conformations in membranes: a fluorescence approach. Biophys. J. 87 (2004) 831-843
    • (2004) Biophys. J. , vol.87 , pp. 831-843
    • Rawat, S.S.1    Kelkar, D.A.2    Chattopadhyay, A.3
  • 45
    • 21244455982 scopus 로고    scopus 로고
    • Effect of graded hydration on the dynamics of an ion channel peptide: a fluorescence approach
    • Kelkar D.A., and Chattopadhyay A. Effect of graded hydration on the dynamics of an ion channel peptide: a fluorescence approach. Biophys. J. 88 (2005) 1070-1080
    • (2005) Biophys. J. , vol.88 , pp. 1070-1080
    • Kelkar, D.A.1    Chattopadhyay, A.2
  • 46
    • 27944498176 scopus 로고    scopus 로고
    • Dynamics of a membrane-bound tryptophan analog in environments of varying hydration: a fluorescence approach
    • Chattopadhyay A., Arora A., and Kelkar D.A. Dynamics of a membrane-bound tryptophan analog in environments of varying hydration: a fluorescence approach. Eur. Biophys. J. 35 (2005) 62-71
    • (2005) Eur. Biophys. J. , vol.35 , pp. 62-71
    • Chattopadhyay, A.1    Arora, A.2    Kelkar, D.A.3
  • 47
    • 25444458922 scopus 로고    scopus 로고
    • Ultrafast hydration dynamics in melittin folding and aggregation: helix formation and tetramer self-assembly
    • Qiu W., Zhang L., Kao Y.-T., Lu W., Li T., Kim J., Sollenberger G.M., Wang L., and Zhong D. Ultrafast hydration dynamics in melittin folding and aggregation: helix formation and tetramer self-assembly. J. Phys. Chem., B 109 (2005) 16901-16910
    • (2005) J. Phys. Chem., B , vol.109 , pp. 16901-16910
    • Qiu, W.1    Zhang, L.2    Kao, Y.-T.3    Lu, W.4    Li, T.5    Kim, J.6    Sollenberger, G.M.7    Wang, L.8    Zhong, D.9
  • 48
    • 0028013531 scopus 로고
    • Peptides in lipid bilayers: structural and thermodynamic basis of partitioning and folding
    • White S.H., and Wimley W.C. Peptides in lipid bilayers: structural and thermodynamic basis of partitioning and folding. Curr. Opin. Struct. Biol. 4 (1994) 79-86
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 79-86
    • White, S.H.1    Wimley, W.C.2
  • 49
    • 0001527174 scopus 로고
    • Wavelength-selective fluorescence as a novel tool to study organization and dynamics in complex biological systems
    • Mukherjee S., and Chattopadhyay A. Wavelength-selective fluorescence as a novel tool to study organization and dynamics in complex biological systems. J. Fluoresc. 5 (1995) 237-246
    • (1995) J. Fluoresc. , vol.5 , pp. 237-246
    • Mukherjee, S.1    Chattopadhyay, A.2
  • 50
    • 0021891880 scopus 로고
    • Time-resolved fluorescence of proteins
    • Beechem J.M., and Brand L. Time-resolved fluorescence of proteins. Annu. Rev. Biochem. 54 (1985) 43-71
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 43-71
    • Beechem, J.M.1    Brand, L.2
  • 51
    • 33947295202 scopus 로고
    • The influence of solvent and temperature upon the fluorescence of indole derivatives
    • Kirby E.P., and Steiner R.F. The influence of solvent and temperature upon the fluorescence of indole derivatives. J. Phys. Chem. 74 (1970) 4480-4490
    • (1970) J. Phys. Chem. , vol.74 , pp. 4480-4490
    • Kirby, E.P.1    Steiner, R.F.2
  • 53
    • 0001917250 scopus 로고
    • Fluorescence quenching: theory and applications
    • Lakowicz J.R. (Ed), Plenum Press, New York
    • Eftink M.R. Fluorescence quenching: theory and applications. In: Lakowicz J.R. (Ed). Topics in Fluorescence Spectroscopy vol. 2 (1991), Plenum Press, New York 53-126
    • (1991) Topics in Fluorescence Spectroscopy , vol.2 , pp. 53-126
    • Eftink, M.R.1
  • 54
    • 0033613815 scopus 로고    scopus 로고
    • Folding of amphipathic α-helices on membranes: energetics of helix formation by melittin
    • Ladokhin A.S., and White S.H. Folding of amphipathic α-helices on membranes: energetics of helix formation by melittin. J. Mol. Biol. 285 (1999) 1363-1369
    • (1999) J. Mol. Biol. , vol.285 , pp. 1363-1369
    • Ladokhin, A.S.1    White, S.H.2
  • 55
    • 0029913459 scopus 로고    scopus 로고
    • Conformational stability and catalytic activity of HIV-1 protease are both enhanced at high salt concentration
    • Szeltner Z., and Polgar L. Conformational stability and catalytic activity of HIV-1 protease are both enhanced at high salt concentration. J. Biol. Chem. 271 (1996) 5458-5463
    • (1996) J. Biol. Chem. , vol.271 , pp. 5458-5463
    • Szeltner, Z.1    Polgar, L.2
  • 56
    • 0034176183 scopus 로고    scopus 로고
    • Electrostatic interactions affecting the active site of class sigma glutathione S-transferase
    • Stevens J.M., Armstrong R.N., and Dirr H.W. Electrostatic interactions affecting the active site of class sigma glutathione S-transferase. Biochem. J. 347 (2000) 193-197
    • (2000) Biochem. J. , vol.347 , pp. 193-197
    • Stevens, J.M.1    Armstrong, R.N.2    Dirr, H.W.3
  • 57
    • 2542457488 scopus 로고    scopus 로고
    • Effect of pH and ionic strength on the cytolytic toxin Cyt1A: a fluorescence spectroscopy study
    • Manceva S.D., Pusztai-Carey M., and Butko P. Effect of pH and ionic strength on the cytolytic toxin Cyt1A: a fluorescence spectroscopy study. Biochim. Biophys. Acta 1699 (2004) 123-130
    • (2004) Biochim. Biophys. Acta , vol.1699 , pp. 123-130
    • Manceva, S.D.1    Pusztai-Carey, M.2    Butko, P.3
  • 59
    • 0344054257 scopus 로고    scopus 로고
    • Monovalent cations differentially affect membrane surface properties and membrane curvature, as revealed by fluorescent probes and dynamic light scattering
    • Kraayenhof R., Sterk G.J., Wong Fong Song H.W., Krab K., and Epand R.M. Monovalent cations differentially affect membrane surface properties and membrane curvature, as revealed by fluorescent probes and dynamic light scattering. Biochim. Biophys. Acta 1282 (1996) 293-302
    • (1996) Biochim. Biophys. Acta , vol.1282 , pp. 293-302
    • Kraayenhof, R.1    Sterk, G.J.2    Wong Fong Song, H.W.3    Krab, K.4    Epand, R.M.5
  • 60
    • 0346756190 scopus 로고    scopus 로고
    • Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature
    • Bigay J., Gounon P., Robineau S., and Antonny B. Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature. Nature 426 (2003) 563-566
    • (2003) Nature , vol.426 , pp. 563-566
    • Bigay, J.1    Gounon, P.2    Robineau, S.3    Antonny, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.