메뉴 건너뛰기




Volumn 117, Issue 10, 2013, Pages 2906-2917

Fluorescence detection of lipid-induced oligomeric intermediates involved in lysozyme "amyloid-like" fiber formation driven by anionic membranes

Author keywords

[No Author keywords available]

Indexed keywords

DYES; FLUORESCENCE; GLYCOPROTEINS; LIPOSOMES; OLIGOMERS; STOICHIOMETRY;

EID: 84875136314     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp310396v     Document Type: Article
Times cited : (8)

References (64)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein Misfolding, Functional Amyloid, and Human Disease
    • Chiti, F.; Dobson, C. M. Protein Misfolding, Functional Amyloid, and Human Disease Annu. Rev. Biochem. 2006, 75, 333-366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 84858374665 scopus 로고    scopus 로고
    • The Amyloid State of Proteins in Human Diseases
    • Eisenberg, D.; Jucker, M. The Amyloid State of Proteins in Human Diseases Cell 2012, 148, 1188-1203
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 5
    • 0344944630 scopus 로고    scopus 로고
    • Protein Aggregation and Aggregate Toxicity: New Insights into Protein Folding, Misfolding Diseases and Biological Evolution
    • Stefani, M.; Dobson, C. M. Protein Aggregation and Aggregate Toxicity: New Insights Into Protein Folding, Misfolding Diseases and Biological Evolution J. Mol. Med. 2003, 81, 678-699
    • (2003) J. Mol. Med. , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 6
    • 33646557678 scopus 로고    scopus 로고
    • The Role of Lipid-Protein Interactions in Amyloid-Type Protein Fibril Formation
    • Gorbenko, G. P.; Kinnunen, P. K. J. The Role of Lipid-Protein Interactions in Amyloid-Type Protein Fibril Formation Chem. Phys. Lipids 2006, 141, 72-82
    • (2006) Chem. Phys. Lipids , vol.141 , pp. 72-82
    • Gorbenko, G.P.1    Kinnunen, P.K.J.2
  • 8
    • 67650325176 scopus 로고    scopus 로고
    • The Interplay of Catalysis and Toxicity by Amyloid Intermediates on Lipid Bilayers: Insights from Type II Diabetes
    • Hebda, J. A.; Miranker, A. D. The Interplay of Catalysis and Toxicity by Amyloid Intermediates on Lipid Bilayers: Insights from Type II Diabetes Ann. Rev. Biophys. 2009, 38, 125-152
    • (2009) Ann. Rev. Biophys. , vol.38 , pp. 125-152
    • Hebda, J.A.1    Miranker, A.D.2
  • 9
    • 0242668337 scopus 로고    scopus 로고
    • Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis
    • Kayed, R.; Head, E.; Thompson, J. L.; McIntire, T. M.; Milton, S. C.; Cotman, C. W.; Glabe, C. G. Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis Science 2003, 300, 486-489
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 10
    • 80053589341 scopus 로고    scopus 로고
    • Membrane and Surface Interactions of Alzheimer's Aβ Peptide - Insights into the Mechanism of Cytotoxicity
    • Williams, T. L.; Serpell, L. C. Membrane and Surface Interactions of Alzheimer's Aβ Peptide-Insights Into the Mechanism of Cytotoxicity FEBS J. 2011, 278, 3905-3917
    • (2011) FEBS J. , vol.278 , pp. 3905-3917
    • Williams, T.L.1    Serpell, L.C.2
  • 11
    • 4043100348 scopus 로고    scopus 로고
    • Formation of Amyloid Fibers Triggered by Phosphatidylserine-Containing Membranes
    • Zhao, H. X.; Tuominen, E. K. J.; Kinnunen, P. K. J. Formation of Amyloid Fibers Triggered by Phosphatidylserine-Containing Membranes Biochemistry 2004, 43, 10302-10307
    • (2004) Biochemistry , vol.43 , pp. 10302-10307
    • Zhao, H.X.1    Tuominen, E.K.J.2    Kinnunen, P.K.J.3
  • 12
    • 14344250143 scopus 로고    scopus 로고
    • Binding of Endostatin to Phosphatidylserine-Containing Membranes and Formation of Amyloid-Like Fibers
    • Zhao, H. X.; Jutila, A.; Nurminen, T.; Wickstrom, S. A.; Keski-Oja, J.; Kinnunen, P. K. J. Binding of Endostatin to Phosphatidylserine-Containing Membranes and Formation of Amyloid-Like Fibers Biochemistry 2005, 44, 2857-2863
    • (2005) Biochemistry , vol.44 , pp. 2857-2863
    • Zhao, H.X.1    Jutila, A.2    Nurminen, T.3    Wickstrom, S.A.4    Keski-Oja, J.5    Kinnunen, P.K.J.6
  • 13
    • 33748942106 scopus 로고    scopus 로고
    • Interaction of the Antimicrobial Peptide Pheromone Plantaricin A with Model Membranes: Implications for a Novel Mechanism of Action
    • Zhao, H.; Sood, R.; Jutila, A.; Bose, S.; Fimland, G.; Nissen-Meyer, J.; Kinnunen, P. K. J. Interaction of the Antimicrobial Peptide Pheromone Plantaricin A with Model Membranes: Implications for a Novel Mechanism of Action Biochim. Biophys. Acta 2006, 1758, 1461-1474
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1461-1474
    • Zhao, H.1    Sood, R.2    Jutila, A.3    Bose, S.4    Fimland, G.5    Nissen-Meyer, J.6    Kinnunen, P.K.J.7
  • 14
    • 33845459710 scopus 로고    scopus 로고
    • Antimicrobial Peptides Temporins B and L Induce Formation of Tubular Lipid Protrusions from Supported Phospholipid Bilayers
    • Domanov, Y. A.; Kinnunen, P. K. J. Antimicrobial Peptides Temporins B and L Induce Formation of Tubular Lipid Protrusions from Supported Phospholipid Bilayers Biophys. J. 2006, 91, 4427-4439
    • (2006) Biophys. J. , vol.91 , pp. 4427-4439
    • Domanov, Y.A.1    Kinnunen, P.K.J.2
  • 15
    • 33847668734 scopus 로고    scopus 로고
    • Fluorescent Temporin B Derivative and Its Binding to Liposomes
    • Sood, R.; Domanov, Y.; Kinnunen, P. K. J. Fluorescent Temporin B Derivative and Its Binding to Liposomes J. Fluoresc. 2007, 17, 223-234
    • (2007) J. Fluoresc. , vol.17 , pp. 223-234
    • Sood, R.1    Domanov, Y.2    Kinnunen, P.K.J.3
  • 17
    • 46749125355 scopus 로고    scopus 로고
    • Amyloid-Type Fiber Formation in Control of Enzyme Action: Interfacial Activation of Phospholipase A(2)
    • Code, C.; Domanov, Y.; Jutila, A.; Kinnunen, P. K. J. Amyloid-Type Fiber Formation in Control of Enzyme Action: Interfacial Activation of Phospholipase A(2) Biophys. J. 2008, 95, 215-224
    • (2008) Biophys. J. , vol.95 , pp. 215-224
    • Code, C.1    Domanov, Y.2    Jutila, A.3    Kinnunen, P.K.J.4
  • 18
    • 65349148494 scopus 로고    scopus 로고
    • Activation of Phospholipase A(2) by Temporin B: Formation of Antimicrobial Peptide-Enzyme Amyloid-Type Cofibrils
    • Code, C.; Domanov, Y. A.; Killian, J. A.; Kinnunen, P. K. J. Activation of Phospholipase A(2) by Temporin B: Formation of Antimicrobial Peptide-Enzyme Amyloid-Type Cofibrils Biochim. Biophys. Acta 2009, 1788, 1064-1072
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1064-1072
    • Code, C.1    Domanov, Y.A.2    Killian, J.A.3    Kinnunen, P.K.J.4
  • 19
    • 39349102682 scopus 로고    scopus 로고
    • The Formation of Amyloid Fibrils from Proteins in the Lysozyme Family
    • Trexler, A. J.; Nilsson, M. R. The Formation of Amyloid Fibrils from Proteins in the Lysozyme Family Curr. Protein Pept. Sci. 2007, 8, 537-557
    • (2007) Curr. Protein Pept. Sci. , vol.8 , pp. 537-557
    • Trexler, A.J.1    Nilsson, M.R.2
  • 22
    • 0035941271 scopus 로고    scopus 로고
    • A Helix-Loop-Helix Peptide at the Upper Lip of the Active Site Cleft of Lysozyme Confers Potent Antimicrobial Activity with Membrane Permeabilization Action
    • Ibrahim, H. R.; Thomas, U.; Pellegrini, A. A Helix-Loop-Helix Peptide at the Upper Lip of the Active Site Cleft of Lysozyme Confers Potent Antimicrobial Activity with Membrane Permeabilization Action J. Biol. Chem. 2001, 276, 43767-43774
    • (2001) J. Biol. Chem. , vol.276 , pp. 43767-43774
    • Ibrahim, H.R.1    Thomas, U.2    Pellegrini, A.3
  • 23
    • 0001256923 scopus 로고    scopus 로고
    • Partially Unfolded Lysozyme at Neutral pH Agglutinates and Kills Gram-Negative and Gram-Positive Bacteria Through Membrane Damage Mechanism
    • Ibrahim, H. R.; Higashiguchi, S.; Koketsu, M.; Juneja, L. R.; Kim, M.; Yamamoto, T.; Sugimoto, Y.; Aoki, T. Partially Unfolded Lysozyme at Neutral pH Agglutinates and Kills Gram-Negative and Gram-Positive Bacteria Through Membrane Damage Mechanism J. Agric. Food Chem. 1996, 44, 3799-3806
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 3799-3806
    • Ibrahim, H.R.1    Higashiguchi, S.2    Koketsu, M.3    Juneja, L.R.4    Kim, M.5    Yamamoto, T.6    Sugimoto, Y.7    Aoki, T.8
  • 24
    • 0035964823 scopus 로고    scopus 로고
    • Genetic Evidence that Antibacterial Activity of Lysozyme Is Independent of Its Catalytic Function
    • Ibrahim, H. R.; Matsuzaki, T.; Aoki, T. Genetic Evidence that Antibacterial Activity of Lysozyme Is Independent of Its Catalytic Function FEBS Lett. 2001, 506, 27-32
    • (2001) FEBS Lett. , vol.506 , pp. 27-32
    • Ibrahim, H.R.1    Matsuzaki, T.2    Aoki, T.3
  • 25
    • 33745303470 scopus 로고    scopus 로고
    • The Peptidoglycan-Degrading Property of Lysozyme Is Not Required for Bactericidal Activity in Vivo
    • Nash, J. A.; Ballard, T. N. S.; Weaver, T. E.; Akinbi, H. T. The Peptidoglycan-Degrading Property of Lysozyme Is Not Required for Bactericidal Activity in Vivo J. Immunol. 2006, 177, 519-526
    • (2006) J. Immunol. , vol.177 , pp. 519-526
    • Nash, J.A.1    Ballard, T.N.S.2    Weaver, T.E.3    Akinbi, H.T.4
  • 26
    • 80051786035 scopus 로고    scopus 로고
    • The Effect of Variable Liposome Brightness on Quantifying Lipid-Protein Interactions Using Fluorescence Correlation Spectroscopy
    • Melo, A. M.; Prieto, M.; Coutinho, A. The Effect of Variable Liposome Brightness on Quantifying Lipid-Protein Interactions Using Fluorescence Correlation Spectroscopy Biochim. Biophys. Acta 2011, 1808, 2559-2568
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 2559-2568
    • Melo, A.M.1    Prieto, M.2    Coutinho, A.3
  • 27
    • 0027233827 scopus 로고
    • The Role of Protein Charge in Protein-Lipid Interactions. pH-Dependent Changes of the Electrophoretic Mobility of Liposomes Through Adsorption of Water-Soluble, Globular Proteins
    • Bergers, J. J.; Vingerhoeds, M. H.; Vanbloois, L.; Herron, J. N.; Janssen, L. H. M.; Fischer, M. J. E.; Crommelin, D. J. A. The Role of Protein Charge in Protein-Lipid Interactions. pH-Dependent Changes of the Electrophoretic Mobility of Liposomes Through Adsorption of Water-Soluble, Globular Proteins Biochemistry 1993, 32, 4641-4649
    • (1993) Biochemistry , vol.32 , pp. 4641-4649
    • Bergers, J.J.1    Vingerhoeds, M.H.2    Vanbloois, L.3    Herron, J.N.4    Janssen, L.H.M.5    Fischer, M.J.E.6    Crommelin, D.J.A.7
  • 29
    • 0034152715 scopus 로고    scopus 로고
    • Association of Lysozyme with Phospholipid Vesicles Is Accompanied by Membrane Surface Dehydration
    • Zschornig, O.; Paasche, G.; Thieme, C.; Korb, N.; Fahrwald, A.; Arnold, K. Association of Lysozyme with Phospholipid Vesicles Is Accompanied by Membrane Surface Dehydration Gen. Physiol. Biophys. 2000, 19, 85-101
    • (2000) Gen. Physiol. Biophys. , vol.19 , pp. 85-101
    • Zschornig, O.1    Paasche, G.2    Thieme, C.3    Korb, N.4    Fahrwald, A.5    Arnold, K.6
  • 30
    • 15244340397 scopus 로고    scopus 로고
    • Modulation of Lysozyme Charge Influences Interaction with Phospholipid Vesicles
    • Zschornig, O.; Paasche, G.; Thieme, C.; Korb, N.; Arnold, K. Modulation of Lysozyme Charge Influences Interaction with Phospholipid Vesicles Colloids Surf., B 2005, 42, 69-78
    • (2005) Colloids Surf., B , vol.42 , pp. 69-78
    • Zschornig, O.1    Paasche, G.2    Thieme, C.3    Korb, N.4    Arnold, K.5
  • 31
    • 84859336807 scopus 로고    scopus 로고
    • Lysozyme Interaction with Negatively Charged Lipid Bilayers: Protein Aggregation and Membrane Fusion
    • Al Kayal, T.; Nappini, S.; Russo, E.; Berti, D.; Bucciantini, M.; Stefani, M.; Baglioni, P. Lysozyme Interaction with Negatively Charged Lipid Bilayers: Protein Aggregation and Membrane Fusion Soft Matter 2012, 8, 4524-4534
    • (2012) Soft Matter , vol.8 , pp. 4524-4534
    • Al Kayal, T.1    Nappini, S.2    Russo, E.3    Berti, D.4    Bucciantini, M.5    Stefani, M.6    Baglioni, P.7
  • 32
    • 84873918586 scopus 로고    scopus 로고
    • Interactions of Lysozyme with Phospholipid Vesicles: Effects of Vesicle Biophysical Features on Protein Misfolding and Aggregation
    • Al Kayal, T.; Russo, E.; Pieri, L.; Caminati, G.; Berti, D.; Bucciantini, M.; Stefani, M.; Baglioni, P. Interactions of Lysozyme with Phospholipid Vesicles: Effects of Vesicle Biophysical Features on Protein Misfolding and Aggregation Soft Matter 2012, 8, 9115-9126
    • (2012) Soft Matter , vol.8 , pp. 9115-9126
    • Al Kayal, T.1    Russo, E.2    Pieri, L.3    Caminati, G.4    Berti, D.5    Bucciantini, M.6    Stefani, M.7    Baglioni, P.8
  • 33
    • 67650069580 scopus 로고    scopus 로고
    • Fluorescence Quenching by Photoinduced Electron Transfer: A Reporter for Conformational Dynamics of Macromolecules
    • Doose, S.; Neuweiler, H.; Sauer, M. Fluorescence Quenching by Photoinduced Electron Transfer: A Reporter for Conformational Dynamics of Macromolecules ChemPhysChem 2009, 10, 1389-1398
    • (2009) ChemPhysChem , vol.10 , pp. 1389-1398
    • Doose, S.1    Neuweiler, H.2    Sauer, M.3
  • 35
    • 79952731301 scopus 로고    scopus 로고
    • Unfolding Dynamics of Cytochrome c Revealed by Single-Molecule and Ensemble-Averaged Spectroscopy
    • Choi, J.; Kim, S.; Tachikawa, T.; Fujitsuka, M.; Majima, T. Unfolding Dynamics of Cytochrome c Revealed by Single-Molecule and Ensemble-Averaged Spectroscopy Phys. Chem. Chem. Phys. 2011, 13, 5651-5658
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 5651-5658
    • Choi, J.1    Kim, S.2    Tachikawa, T.3    Fujitsuka, M.4    Majima, T.5
  • 40
    • 0028871804 scopus 로고
    • How to Measure and Predict the Molar Absorption Coefficient of a Protein
    • Pace, C. N.; Vajdos, F.; Fee, L.; Grimsley, G.; Gray, T. How to Measure and Predict the Molar Absorption Coefficient of a Protein Protein Sci. 1995, 4, 2411-2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 41
    • 0015019307 scopus 로고
    • An Accurate and Convenient Organic Phosphorus Assay
    • McClare, C. W. F. An Accurate and Convenient Organic Phosphorus Assay Anal. Biochem. 1971, 39, 527-530
    • (1971) Anal. Biochem. , vol.39 , pp. 527-530
    • McClare, C.W.F.1
  • 42
    • 58149288322 scopus 로고    scopus 로고
    • Pinched Multilamellar Structure of Aggregates of Lysozyme and Phosphatidylserine-Containing Membranes Revealed by FRET
    • Coutinho, A.; Loura, L. M. S.; Fedorov, A.; Prieto, M. Pinched Multilamellar Structure of Aggregates of Lysozyme and Phosphatidylserine- Containing Membranes Revealed by FRET Biophys. J. 2008, 95, 4726-4736
    • (2008) Biophys. J. , vol.95 , pp. 4726-4736
    • Coutinho, A.1    Loura, L.M.S.2    Fedorov, A.3    Prieto, M.4
  • 43
    • 0032321726 scopus 로고    scopus 로고
    • Protein Folding in Membranes: Determining Energetics of Peptide-Bilayer Interactions
    • White, S. H.; Wimley, W. C.; Ladokhin, A. S.; Hristova, K. Protein Folding in Membranes: Determining Energetics of Peptide-Bilayer Interactions Methods Enzymol. 1998, 295, 62-87
    • (1998) Methods Enzymol. , vol.295 , pp. 62-87
    • White, S.H.1    Wimley, W.C.2    Ladokhin, A.S.3    Hristova, K.4
  • 44
    • 0030043562 scopus 로고    scopus 로고
    • Surface Areas and Packing Constraints in POPC/C(12)EO(n) Membranes. A Time-Resolved Fluorescence Study
    • Lantzsch, G.; Binder, H.; Heerklotz, H.; Wendling, M.; Klose, G. Surface Areas and Packing Constraints in POPC/C(12)EO(n) Membranes. A Time-Resolved Fluorescence Study Biophys. Chem. 1996, 58, 289-302
    • (1996) Biophys. Chem. , vol.58 , pp. 289-302
    • Lantzsch, G.1    Binder, H.2    Heerklotz, H.3    Wendling, M.4    Klose, G.5
  • 45
    • 77958474675 scopus 로고    scopus 로고
    • Consistent Picture of the Reversible Thermal Unfolding of Hen Egg-White Lysozyme from Experiment and Molecular Dynamics
    • Meersman, F.; Atilgan, C.; Miles, A. J.; Bader, R.; Shang, W. F.; Matagne, A.; Wallace, B. A.; Koch, M. H. J. Consistent Picture of the Reversible Thermal Unfolding of Hen Egg-White Lysozyme from Experiment and Molecular Dynamics Biophys. J. 2010, 99, 2255-2263
    • (2010) Biophys. J. , vol.99 , pp. 2255-2263
    • Meersman, F.1    Atilgan, C.2    Miles, A.J.3    Bader, R.4    Shang, W.F.5    Matagne, A.6    Wallace, B.A.7    Koch, M.H.J.8
  • 46
    • 0026625689 scopus 로고
    • Protein Surface Topology-Probing by Selective Chemical Modification and Mass Spectrometric Peptide Mapping
    • Suckau, D.; Mak, M.; Przybylski, M. Protein Surface Topology-Probing by Selective Chemical Modification and Mass Spectrometric Peptide Mapping Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 5630-5634
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 5630-5634
    • Suckau, D.1    Mak, M.2    Przybylski, M.3
  • 47
    • 34548277682 scopus 로고    scopus 로고
    • Changes in Retention Behavior of Fluorescently Labeled Proteins during Ion-Exchange Chromatography Caused by Different Protein Surface Labeling Positions
    • Teske, C. A.; Simon, R.; Niebisch, A.; Hubbuch, J. Changes in Retention Behavior of Fluorescently Labeled Proteins During Ion-Exchange Chromatography Caused by Different Protein Surface Labeling Positions Biotechnol. Bioeng. 2007, 98, 193-200
    • (2007) Biotechnol. Bioeng. , vol.98 , pp. 193-200
    • Teske, C.A.1    Simon, R.2    Niebisch, A.3    Hubbuch, J.4
  • 48
    • 34447291808 scopus 로고    scopus 로고
    • Binding of Lysozyme to Phospholipid Bilayers: Evidence for Protein Aggregation Upon Membrane Association
    • Gorbenko, G. P.; Ioffe, V. M.; Kinnunen, P. K. J. Binding of Lysozyme to Phospholipid Bilayers: Evidence for Protein Aggregation Upon Membrane Association Biophys. J. 2007, 93, 140-153
    • (2007) Biophys. J. , vol.93 , pp. 140-153
    • Gorbenko, G.P.1    Ioffe, V.M.2    Kinnunen, P.K.J.3
  • 50
    • 0028801883 scopus 로고
    • Protein Surface-Distribution and Protein-Protein Interactions in the Binding of Peripheral Proteins to Charged Lipid Membranes
    • Heimburg, T.; Marsh, D. Protein Surface-Distribution and Protein-Protein Interactions in the Binding of Peripheral Proteins to Charged Lipid Membranes Biophys. J. 1995, 68, 536-546
    • (1995) Biophys. J. , vol.68 , pp. 536-546
    • Heimburg, T.1    Marsh, D.2
  • 51
    • 0033031748 scopus 로고    scopus 로고
    • Binding of Peripheral Proteins to Mixed Lipid Membranes: Effect of Lipid Demixing Upon Binding
    • Heimburg, T.; Angerstein, B.; Marsh, D. Binding of Peripheral Proteins to Mixed Lipid Membranes: Effect of Lipid Demixing Upon Binding Biophys. J. 1999, 76, 2575-2586
    • (1999) Biophys. J. , vol.76 , pp. 2575-2586
    • Heimburg, T.1    Angerstein, B.2    Marsh, D.3
  • 52
    • 0035827137 scopus 로고    scopus 로고
    • Protein Chemistry at Membrane Interfaces: Non-Additivity of Electrostatic and Hydrophobic Interactions
    • Ladokhin, A. S.; White, S. H. Protein Chemistry at Membrane Interfaces: Non-Additivity of Electrostatic and Hydrophobic Interactions J. Mol. Biol. 2001, 309, 543-552
    • (2001) J. Mol. Biol. , vol.309 , pp. 543-552
    • Ladokhin, A.S.1    White, S.H.2
  • 53
    • 7044235790 scopus 로고    scopus 로고
    • Thermodynamics of Lipid-Peptide Interactions
    • Seelig, J. Thermodynamics of Lipid-Peptide Interactions Biochim. Biophys. Acta 2004, 1666, 40-50
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 40-50
    • Seelig, J.1
  • 54
    • 41049083881 scopus 로고    scopus 로고
    • Confocal Laser Scanning Microscopy as an Analytical Tool in Chromatographic Research
    • Hubbuch, J.; Kula, M. R. Confocal Laser Scanning Microscopy as an Analytical Tool in Chromatographic Research Bioprocess Biosyst. Eng. 2008, 31, 241-259
    • (2008) Bioprocess Biosyst. Eng. , vol.31 , pp. 241-259
    • Hubbuch, J.1    Kula, M.R.2
  • 55
    • 65249093640 scopus 로고    scopus 로고
    • Thermodynamics of Melittin Binding to Lipid Bilayers. Aggregation and Pore Formation
    • Klocek, G.; Schulthess, T.; Shai, Y.; Seelig, J. Thermodynamics of Melittin Binding to Lipid Bilayers. Aggregation and Pore Formation Biochemistry 2009, 48, 2586-2596
    • (2009) Biochemistry , vol.48 , pp. 2586-2596
    • Klocek, G.1    Schulthess, T.2    Shai, Y.3    Seelig, J.4
  • 56
    • 0029970884 scopus 로고    scopus 로고
    • Adsorption of Globular Proteins on Locally Planar Surfaces: Models for the Effect of Excluded Surface Area and Aggregation of Adsorbed Protein on Adsorption Equilibria
    • Chatelier, R. C.; Minton, A. P. Adsorption of Globular Proteins on Locally Planar Surfaces: Models for the Effect of Excluded Surface Area and Aggregation of Adsorbed Protein on Adsorption Equilibria Biophys. J. 1996, 71, 2367-2374
    • (1996) Biophys. J. , vol.71 , pp. 2367-2374
    • Chatelier, R.C.1    Minton, A.P.2
  • 57
    • 0032905175 scopus 로고    scopus 로고
    • Adsorption of Globular Proteins on Locally Planar Surfaces. II. Models for the Effect of Multiple Adsorbate Conformations on Adsorption Equilibria and Kinetics
    • Minton, A. P. Adsorption of Globular Proteins on Locally Planar Surfaces. II. Models for the Effect of Multiple Adsorbate Conformations on Adsorption Equilibria and Kinetics Biophys. J. 1999, 76, 176-187
    • (1999) Biophys. J. , vol.76 , pp. 176-187
    • Minton, A.P.1
  • 58
    • 0034753275 scopus 로고    scopus 로고
    • Insertion and Pore Formation Driven by Adsorption of Proteins onto Lipid Bilayer Membrane-Water Interfaces
    • Zuckermann, M. J.; Heimburg, T. Insertion and Pore Formation Driven by Adsorption of Proteins Onto Lipid Bilayer Membrane-Water Interfaces Biophys. J. 2001, 81, 2458-2472
    • (2001) Biophys. J. , vol.81 , pp. 2458-2472
    • Zuckermann, M.J.1    Heimburg, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.