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Kinnunen, P.K.J.1
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0344867883
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Correlation between protein kinase C α activity and membrane phase behavior
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This work illustrates the extent to which lipid dispersions must be characterized in order to relate structure and function. The authors show that, at 30 mol% diacylglycerol (the composition corresponding to that of compound formation with the phospholipids), the activity of a protein kinase C isoform is maximal
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Micol V, Sánchez-Piñera P, Villalain J, de Godos A, Gómez-Fernández JC: Correlation between protein kinase C α activity and membrane phase behavior. Biophys J 1999, 76:916-927. This work illustrates the extent to which lipid dispersions must be characterized in order to relate structure and function. The authors show that, at 30 mol% diacylglycerol (the composition corresponding to that of compound formation with the phospholipids), the activity of a protein kinase C isoform is maximal.
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Micol, V.1
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Interpretation of mechanochemical properties of lipid bilayer vesicles from the equation of state of pressure-area measurement of the monolayer at the air-water or oil-water interface
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This is the most recent in a series of papers that relates the thermodynamic properties of monolayers and bilayers. The focus of these papers has been to define a bilayer equivalent to surface pressure. This effort provides a good review of past developments and concludes that phospholipid molecules in monolayers at collapse and in bilayers at equilibrium with the molecules are not only at the same chemical potential, but also have the same molecular area
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Feng S: Interpretation of mechanochemical properties of lipid bilayer vesicles from the equation of state of pressure-area measurement of the monolayer at the air-water or oil-water interface. Langmuir 1999, 15:998-1010. This is the most recent in a series of papers that relates the thermodynamic properties of monolayers and bilayers. The focus of these papers has been to define a bilayer equivalent to surface pressure. This effort provides a good review of past developments and concludes that phospholipid molecules in monolayers at collapse and in bilayers at equilibrium with the molecules are not only at the same chemical potential, but also have the same molecular area.
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Characterization of the growth of 2D protein crystals on a lipid monolayer by ellipsometry and rigidity measurements coupled to electron microscopy
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Vénien-Bryan C, Lenne P-F, Zakri C, Renault A, Brisson A, Legrand J-F. BErge B: Characterization of the growth of 2D protein crystals on a lipid monolayer by ellipsometry and rigidity measurements coupled to electron microscopy. Biophys J 1998, 74:2649-2657.
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Two-dimensional crystallization of proteins on lipid monolayers at the air-water interface and transfer to an electron microscopy grid
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Brisson A, Bergsma-Schutter W, Oling F, Lambert O, Reviakine I: Two-dimensional crystallization of proteins on lipid monolayers at the air-water interface and transfer to an electron microscopy grid. J Cryst Growth 1999, 196:456-470.
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0033555185
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Penetration of glucose oxidase and of the hydrophobically modified enzyme into phospholipid and cholesterol monolayers
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Baszkin A, Boissonnade MM, Rosilio V, KAmyshny A, Magdassi S: Penetration of glucose oxidase and of the hydrophobically modified enzyme into phospholipid and cholesterol monolayers. J Colloid Interface Sci 1999, 209:302-311.
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0031597411
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2+ independent interaction of annexin I with phospholipid monolayers
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Surface pressure changes in monolayers were used to show that annexin I, but not annexin V, was able to interact with monolayers in the absence of calcium at pH 6.0, but not at pH 7.4. At pH 6.0, calcium changed the kinetics of the interaction, suggesting a calcium-dependent change in conformation
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2+ independent interaction of annexin I with phospholipid monolayers. FEBS Lett 1998, 438:279-284. Surface pressure changes in monolayers were used to show that annexin I, but not annexin V, was able to interact with monolayers in the absence of calcium at pH 6.0, but not at pH 7.4. At pH 6.0, calcium changed the kinetics of the interaction, suggesting a calcium-dependent change in conformation.
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Rosengarth, A.1
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0032055389
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Vidai P, Chaloin L, Heitz A, Van Mau N, Méry J, Divita G, Heitz F: Interactions of primary amphipathic vector peptides with membranes. Conformational consequences and influence on cellular localization. J Membr Biol 1998, 162:259-264.
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Vidai, P.1
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Méry, J.5
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Heitz, F.7
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12
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0032952095
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j(i = 2j) peptides
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This study combines measurements of surface area at constant surface pressure with polarization modulation IR spectroscopy to characterize peptide interactions with lipid monolayers. Peptides from five to nine residues in length form intramolecular antiparallel β sheets, whereas longer peptides form amphipathic α helices. These helices lie flat in the interface and their orientation is not influenced by surface pressure. An unexpected observation was that the affinity of the helices for the interface did not increase with increasing peptide length, but was at its maximum at a length of 12 residues. The product of the calculated hydrophobic moment for the peptide and its molecular areas at the interface correlated with lytic activity over three orders of magnitude
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j(i = 2j) peptides. Biochim Biophys Acta 1999, 1416:176-194. This study combines measurements of surface area at constant surface pressure with polarization modulation IR spectroscopy to characterize peptide interactions with lipid monolayers. Peptides from five to nine residues in length form intramolecular antiparallel β sheets, whereas longer peptides form amphipathic α helices. These helices lie flat in the interface and their orientation is not influenced by surface pressure. An unexpected observation was that the affinity of the helices for the interface did not increase with increasing peptide length, but was at its maximum at a length of 12 residues. The product of the calculated hydrophobic moment for the peptide and its molecular areas at the interface correlated with lytic activity over three orders of magnitude.
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Biochim Biophys Acta
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Momsen WE, Brockman HL: Recovery of monomolecular films in studies of lipolysis. Methods Enzymol 1997, 286:292-305.
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Brockman, H.L.2
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0032499653
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How colipase-fatty acid interactions mediate adsorption of pancreatic lipase to interfaces
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This study addresses the role of pancreatic lipase fatty acid product in regulating the ability of the lipase cofactor protein, colipase, to serve as a binding locus for lipase. An unexpected finding was that the presence of colipase in a phosphatidylcholine monolayer was not sufficient for lipase adsorption. Rather, the presence of the fatty acid was also needed and lipase binding increased exponentially with increasing amounts of fatty acid. Consideration of these observations in light of the ability of colipase to laterally recruit lipase substrates and products in the interface leads to a new paradigm for how colipase facilitates lipolysis. This paper illustrates how a complex problem can be addressed with relatively simple methods
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Dahim M, Momsen WE, Brockman HL: How colipase-fatty acid interactions mediate adsorption of pancreatic lipase to interfaces. Biochemistry 1998, 37:8369-8377. This study addresses the role of pancreatic lipase fatty acid product in regulating the ability of the lipase cofactor protein, colipase, to serve as a binding locus for lipase. An unexpected finding was that the presence of colipase in a phosphatidylcholine monolayer was not sufficient for lipase adsorption. Rather, the presence of the fatty acid was also needed and lipase binding increased exponentially with increasing amounts of fatty acid. Consideration of these observations in light of the ability of colipase to laterally recruit lipase substrates and products in the interface leads to a new paradigm for how colipase facilitates lipolysis. This paper illustrates how a complex problem can be addressed with relatively simple methods.
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Biochemistry
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Dahim, M.1
Momsen, W.E.2
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Peptide-lipid interactions in Langmuir monolayers at the air/water interface. A novel thermodynamic analysis of a two-component surfactant system
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Schwarz G, Taylor SE: Peptide-lipid interactions in Langmuir monolayers at the air/water interface. A novel thermodynamic analysis of a two-component surfactant system. Supramol Sci 1997, 4:479-483.
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Welzel PB, Weis I, Schwarz G: Sources of error in Langmuir trough measurements, Wilhelmy plate effects and surface curvature. Colloid Surf A 1998, 144:229-234.
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0032581014
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Conformation and lipid binding properties of four peptides derived from the membrane-binding domain of CTP-phosphocholine cytidylyltransferase
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Protein-induced changes in surface pressure were used to compare peptides derived from the putative membrane-binding domain of phosphocholine cytidylyltransferase. The results show that the peptides are strongly surface active and that the serine residues that interrupt the apolar side of the amphipathic helices lower its affinity for lipid. It is concluded that this lowering of affinity increases the specificity of the peptide-membrane interaction for anionic phospholipids
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Johnson JE, Rao NM, Hui S-W, Cornell RB: Conformation and lipid binding properties of four peptides derived from the membrane-binding domain of CTP-phosphocholine cytidylyltransferase. Biochemistry 1998, 37:9509-9519. Protein-induced changes in surface pressure were used to compare peptides derived from the putative membrane-binding domain of phosphocholine cytidylyltransferase. The results show that the peptides are strongly surface active and that the serine residues that interrupt the apolar side of the amphipathic helices lower its affinity for lipid. It is concluded that this lowering of affinity increases the specificity of the peptide-membrane interaction for anionic phospholipids.
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Biochemistry
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Johnson, J.E.1
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0033593350
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Apolipoprotein-mediated plasma membrane microsolubilization. Role of lipid affinity and membrane penetration in the efflux of cellular cholesterol and phospholipid
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Several apolipoproteins are able to solubilize plasma membrane constituents from cell plasma membranes. A large number of peptides derived from these proteins were obtained and tested for their ability both to solubilize membranes and to increase the surface pressure of egg phosphatidylcholine monolayers. There was a direct correlation between solubilizing ability and monolayer exclusion pressure. This showed that the insertion of the amphipathic helices into the plasma membrane is a required step for peptide solubilization
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Gillotte KL, Zaiou M, Lund-Katz S, Anantharamaiah GM, Holvoet P, Dhoest A, Palgunachari MN, Segrest JP, Weisgraber KH, Rothblat GH, Phillips MC: Apolipoprotein-mediated plasma membrane microsolubilization. Role of lipid affinity and membrane penetration in the efflux of cellular cholesterol and phospholipid. J Biol Chem 1999, 274:2021-2028. Several apolipoproteins are able to solubilize plasma membrane constituents from cell plasma membranes. A large number of peptides derived from these proteins were obtained and tested for their ability both to solubilize membranes and to increase the surface pressure of egg phosphatidylcholine monolayers. There was a direct correlation between solubilizing ability and monolayer exclusion pressure. This showed that the insertion of the amphipathic helices into the plasma membrane is a required step for peptide solubilization.
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Dhoest, A.6
Palgunachari, M.N.7
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Weisgraber, K.H.9
Rothblat, G.H.10
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This study compares the interaction of the effector domain of MARCKS and related proteins with both lipid monolayers and lipid bilayers. Comparable results are obtained that show that both electrostatic and hydrophobic interactions are involved. The simultaneous area dilation and boundary potentials measured in the monolayer system showed that the binding of the peptides to the interface is temporally associated with their insertion among the lipid molecules
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Bähr G, Diederich A, Vergères G, Winterhalter M: Interaction of the effector domain of MARCKS and MARCKS-related protein with lipid membranes revealed by electric potential measurements. Biochemistry 1998, 37:16252-16261. This study compares the interaction of the effector domain of MARCKS and related proteins with both lipid monolayers and lipid bilayers. Comparable results are obtained that show that both electrostatic and hydrophobic interactions are involved. The simultaneous area dilation and boundary potentials measured in the monolayer system showed that the binding of the peptides to the interface is temporally associated with their insertion among the lipid molecules.
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Adjuvant lipopeptide interaction with model membranes
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Both surface pressure and boundary potential measurements were used to characterize the interaction of an acylated peptide with anionic lipid monolayers. The data showed that the ionic strength and lipid species regulated the kinetics of association, but not the end point
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Binding of basic peptides to membranes produces lateral domains enriched in the acidic lipids phosphatidylserine and phosphatidylinositol 4,5-bisphosphate: An electrostatic model and experimental results
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This paper demonstrates the formation of lipid domains in large bilayer membranes, as a consequence of the interaction of anionic phospholipid species with a polycationic MARCKS-related peptide. Although not a monolayer paper, this paper shows how domain formation can be mathematically modeled in either monolayers or bilayers
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Denisov G, Wanaski S, Luan P, Glaser M, McLaughlin S: Binding of basic peptides to membranes produces lateral domains enriched in the acidic lipids phosphatidylserine and phosphatidylinositol 4,5-bisphosphate: An electrostatic model and experimental results. Biophys J 1998, 74:731-744. This paper demonstrates the formation of lipid domains in large bilayer membranes, as a consequence of the interaction of anionic phospholipid species with a polycationic MARCKS-related peptide. Although not a monolayer paper, this paper shows how domain formation can be mathematically modeled in either monolayers or bilayers.
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Vibrational spectroscopic studies of lipid domains in biomembranes and model systems
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This paper presents the theory and application of IR spectroscopy in the detection of lipid domains in model and biological membranes. It provides a well-balanced discussion of both the strengths and the limitations of the approach
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Mendelsohn R, Moore DJ: Vibrational spectroscopic studies of lipid domains in biomembranes and model systems. Chem Phys Lipids 1998, 96:141-157. This paper presents the theory and application of IR spectroscopy in the detection of lipid domains in model and biological membranes. It provides a well-balanced discussion of both the strengths and the limitations of the approach.
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(1998)
Chem Phys Lipids
, vol.96
, pp. 141-157
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Mendelsohn, R.1
Moore, D.J.2
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44
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11544346424
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Infrared spectroscopy of aqueous biophysical monolayers
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Polarized IR spectroscopy of monolayers of phospholipids and lung surfactant proteins were obtained. The paper illustrates nicely the use of this approach in identifying domains of ordered and disordered lipid, and the advantages of deuterium labeling of phospholipid acyl chains for monitoring the state of individual species in a lipid mixture. The results show that surfactant proteins B and C disorder the acyl chains of dipalmitoylphosphatidylcholine, the zwitterionic lipid in the monolayers, but order dioleoylphosphatidylglycerol, the anionic component
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Dluhy RA, Ping Z, Faucher K, Brockman JM: Infrared spectroscopy of aqueous biophysical monolayers. Thin Solid Films 1998, 329:308-314. Polarized IR spectroscopy of monolayers of phospholipids and lung surfactant proteins were obtained. The paper illustrates nicely the use of this approach in identifying domains of ordered and disordered lipid, and the advantages of deuterium labeling of phospholipid acyl chains for monitoring the state of individual species in a lipid mixture. The results show that surfactant proteins B and C disorder the acyl chains of dipalmitoylphosphatidylcholine, the zwitterionic lipid in the monolayers, but order dioleoylphosphatidylglycerol, the anionic component.
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(1998)
Thin Solid Films
, vol.329
, pp. 308-314
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Dluhy, R.A.1
Ping, Z.2
Faucher, K.3
Brockman, J.M.4
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45
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0032212963
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Infrared spectroscopy of supported lipid monolayer, bilayer, and multibilayer membranes
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The approach outlined in this paper is a hybrid between using freestanding monolayers and using monolayers formed by vesicle fusion. Starting with a defined monolayer, it avoids many of the problems of vesicle adherence and partial fusion that are inherent in the fusion method. At the same time, it provides control over lipid-packing density in the film. The comparison shown in this paper supports the notion that monolayers are a reasonable model for half of a bilayer
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Silvestro L, Axelsen PH: Infrared spectroscopy of supported lipid monolayer, bilayer, and multibilayer membranes. Chem Phys Lipids 1998, 96:69-80. The approach outlined in this paper is a hybrid between using freestanding monolayers and using monolayers formed by vesicle fusion. Starting with a defined monolayer, it avoids many of the problems of vesicle adherence and partial fusion that are inherent in the fusion method. At the same time, it provides control over lipid-packing density in the film. The comparison shown in this paper supports the notion that monolayers are a reasonable model for half of a bilayer.
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(1998)
Chem Phys Lipids
, vol.96
, pp. 69-80
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Silvestro, L.1
Axelsen, P.H.2
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47
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0032951122
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Palmitoylation of lung surfactant protein SP-C alters surface thermodynamics, but not protein secondary structure or orientation in 1,2-dipalmitoylphosphatidylcholine Langmuir films
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Flach CR, Gericke A, Keough KMW, Mendelsohn R: Palmitoylation of lung surfactant protein SP-C alters surface thermodynamics, but not protein secondary structure or orientation in 1,2-dipalmitoylphosphatidylcholine Langmuir films. Biochim Biophys Acta 1999, 1416:11-20.
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(1999)
Biochim Biophys Acta
, vol.1416
, pp. 11-20
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Flach, C.R.1
Gericke, A.2
Keough, K.M.W.3
Mendelsohn, R.4
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48
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10644279571
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Use of internal reflectance infrared spectroscopy for the in-situ study of supported lipid monolayers
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Axelsen PD, Braddock WD, Brockman HL, Jones CM, Dluhy RA, Kaufman BS, Puga FJ: Use of internal reflectance infrared spectroscopy for the in-situ study of supported lipid monolayers. Appl Spectrosc 1995, 49:526-531.
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(1995)
Appl Spectrosc
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Axelsen, P.D.1
Braddock, W.D.2
Brockman, H.L.3
Jones, C.M.4
Dluhy, R.A.5
Kaufman, B.S.6
Puga, F.J.7
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49
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0031754538
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A spreading technique for forming film in a captive bubble
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This paper describes modifications of a clever technique for spreading a monolayer on the surface of a captive bubble. The compression and decompression of the chamber containing the bubble controls the surface area and shape, and allows the determination of surface pressure. The authors appear to have overcome many of the earlier limitations of this technique, thereby widening its applicability
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Putz G, Walch M, Van Eijk M, Haagsman HP: A spreading technique for forming film in a captive bubble. Biophys J 1998, 75:2229-2239. This paper describes modifications of a clever technique for spreading a monolayer on the surface of a captive bubble. The compression and decompression of the chamber containing the bubble controls the surface area and shape, and allows the determination of surface pressure. The authors appear to have overcome many of the earlier limitations of this technique, thereby widening its applicability.
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(1998)
Biophys J
, vol.75
, pp. 2229-2239
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Putz, G.1
Walch, M.2
Van Eijk, M.3
Haagsman, H.P.4
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50
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0032575107
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A miniaturized monolayer trough with variable surface area in the square-millimeter range
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Duschl C, Boncheva M, Vogel H: A miniaturized monolayer trough with variable surface area in the square-millimeter range. Biochim Biophys Acta 1998, 1371:345-350.
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(1998)
Biochim Biophys Acta
, vol.1371
, pp. 345-350
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Duschl, C.1
Boncheva, M.2
Vogel, H.3
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51
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0001513686
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Design and performance of an integrated fluorescence, polarized fluorescence, and Brewster angle microscope/Langmuir trough assembly for the study of lung surfactant monolayers
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Lipp MM, Lee KYC, Zasadzinski JA, Waring AJ: Design and performance of an integrated fluorescence, polarized fluorescence, and Brewster angle microscope/Langmuir trough assembly for the study of lung surfactant monolayers. Rev Sci Instr 1997, 68:2574-2582.
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(1997)
Rev Sci Instr
, vol.68
, pp. 2574-2582
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Lipp, M.M.1
Lee, K.Y.C.2
Zasadzinski, J.A.3
Waring, A.J.4
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52
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0001260473
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Surface potential studies using Kelvin force spectroscopy
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Lü J, Guggisberg M, Lüthi R, Kubon M, Scandella L, Gerber C, Meyer E, Güntherodt HJ: Surface potential studies using Kelvin force spectroscopy. Appl Phys A 1998, 66:S273-S275.
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(1998)
Appl Phys A
, vol.66
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Lü, J.1
Guggisberg, M.2
Lüthi, R.3
Kubon, M.4
Scandella, L.5
Gerber, C.6
Meyer, E.7
Güntherodt, H.J.8
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53
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0031997948
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Imaging the molecular dimensions and oligomerization of proteins at liquid/solid interfaces
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Waner MJ, Gilchrist M, Schindler M, Dantus M: Imaging the molecular dimensions and oligomerization of proteins at liquid/solid interfaces. J Phys Chem B: Mat Surf Interfaces Biophys 1998, 102:1649-1657.
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(1998)
J Phys Chem B: Mat Surf Interfaces Biophys
, vol.102
, pp. 1649-1657
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Waner, M.J.1
Gilchrist, M.2
Schindler, M.3
Dantus, M.4
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54
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0032109121
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A compact fluorescence and polarization near-field scanning optical microscope
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Merritt G, Monson E, Betzig E, Kopelman R: A compact fluorescence and polarization near-field scanning optical microscope. Rev Sci Instr 1998, 69:2685-2690.
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(1998)
Rev Sci Instr
, vol.69
, pp. 2685-2690
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Merritt, G.1
Monson, E.2
Betzig, E.3
Kopelman, R.4
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55
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0031835569
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Submicron structure in L-·-dipalmitoylphosphatidylcholine monolayers and bilayers probed with confocal, atomic force, and near-field microscopy
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Hollars CW, Dunn RC: Submicron structure in L-·-dipalmitoylphosphatidylcholine monolayers and bilayers probed with confocal, atomic force, and near-field microscopy. Biophys J 1998, 75:342-353.
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(1998)
Biophys J
, vol.75
, pp. 342-353
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Hollars, C.W.1
Dunn, R.C.2
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56
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85030364709
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NSOM studies of DPPC monolayers at the air/water interface
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in press. Near-field scanning optical microscopy provides data similar to that from epifluorescence imaging, but with resolution of the domain structure on the submicron scale. This paper reports the extension of the technique from supported monolayers (see [55]) to spread monolayers at the air-2M sucrose interface. Importantly, the results show that domain substructures, observed in lipid monolayers transferred onto a solid support and imaged in air [55], are absent when the monolayer is imaged in situ. Moreover, data are presented showing that true imaging at the air-water interface should be possible if an interferometric feedback method is used to control the tip height and perturbation of the lipid monolayer by the tip
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Shiku H, Dunn RC: NSOM studies of DPPC monolayers at the air/water interface. J Microsc 1999, in press. Near-field scanning optical microscopy provides data similar to that from epifluorescence imaging, but with resolution of the domain structure on the submicron scale. This paper reports the extension of the technique from supported monolayers (see [55]) to spread monolayers at the air-2M sucrose interface. Importantly, the results show that domain substructures, observed in lipid monolayers transferred onto a solid support and imaged in air [55], are absent when the monolayer is imaged in situ. Moreover, data are presented showing that true imaging at the air-water interface should be possible if an interferometric feedback method is used to control the tip height and perturbation of the lipid monolayer by the tip.
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(1999)
J Microsc
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Shiku, H.1
Dunn, R.C.2
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