Biophysical Society

FIG. 7 Electron micrograph of cationic lipid/DNA complexes (example of striated lamellae). (Reprinted from Ref. 117, copyright 1999 Biophysical Society.)... 

Figure 5.14 Freeze-etch electron micrograph of glycolipid nanotubes from 24 1 nonhydroxy galactocerebrosides (21) cryofixed from room temperature in water. Bar = 250 nm. Reprinted from Ref. 64 with permission of the Biophysical Society.

Figure 2. This figure gives a schematic illustration of various fluctuations that exist in lipid bilayers. From top to bottom (1) the increase in area and concomitant reduction in membrane thickness is strongly damped. (2) Up and down movements of the lipids are restricted to small amplitudes, i.e. much less than the tail length. (3) Interpenetration of lipids into the opposite monolayer is, in first approximation, forbidden. (4) Conformations of the lipid tails have only few gauche defects, so that the tail is only slightly curved. Reproduced from (58) with permission from the Biophysical Society...

Figure 3 (Plate 2). Representation of molecular structure in MD simulations. Shown here is the SOPC lipid, discussed in the text. The numbers at each atom indicate the partial charge on the atom. The space-filling picture on the left gives insight into the van der Waals radii of the various groups, and thus into the shape of the molecule. Reproduced from (58) with permission from the Biophysical Society...

Figure 5. Profiles across the bilayer of the total lipid density of DPPC, the water density and the densities of certain lipid groups as obtained from MD simulations by Berger et al. [58]. The profiles are found by taking the time average over the last 300 ps of the simulation. The densities for the lipid head-group components are only shown on one side for clarity. The origin of the z-axis is arbitrarily positioned on the left of the bilayer. On the y-axis, the atom density in atoms per nm3 is given. Redrawn from [58] by permission of the Biophysical Society...

Figure 6. V ariation of the orientational order parameter 5 along the hydrocarbon chains of the lipids of DMPC lipid bilayers, according to MD simulations of Berger et al. [58]. The line is drawn to guide the eye. The spheres are experimental values obtained by Seelig and Seelig [59] using 2H-NMR spectroscopy. (Numbering of C-atoms from the head group to the CH3 terminal group). Redrawn from [58] by permission of the Biophysical Society...

Figure 8 (Plate 4). Typical snapshot of DPD simulation results [64]. The hydrophobic part of mixed bilayers of DPPC-like lipids and up to 0.8 mole-fraction of the non-ionic surfactant Ci2E6 (left) and 0.9 (right). The surfactant C]2 chains are represented by grey curves, and the lipid C15 chains are black. The hole in the left conformation is transient on the right they are stable. Reproduced by permission of the Biophysical Society...

KcsA, as used by Shrivastava et al. [168], The channel consists of four peptide chains (for clarity in the picture only two are given), and is embedded in a lipid bilayer. The structure can be thought of as being made up of a selectivity filter, a central cavity, and a gate at the inner side of the bilayer, (b) Water molecules and K+ ions in the selectivity filter SO represents the extracellular mouth. From [168]. Reproduced by permission of the Biophysical Society... 

Figure 2.39 Schematic illustration of cell-cell and cell-substrate adhesion. Reprinted, by permission, from BiophysicalJournal, 45, 1051. Copyright 1984 by the Biophysical Society.

I would like to extend Prof. Simon s characterizations of these beautiful new molecules to include a description of the effects on lipid bilayers of his Na+ selective compound number 11, which my post-doctoral student, Kun-Hung Kuo, and I have found to induce an Na+ selective permeation across lipid bilayer membranes [K.-H. Kuo and G. Eisenman, Naf Selective Permeation of Lipid Bilayers, mediated by a Neutral Ionophore, Abstracts 21st Nat. Biophysical Society meeting (Biophys. J., 17, 212a (1977))]. This is the first example, to my knowledge, of the successful reconstitution of an Na+ selective permeation in an artificial bilayer system. (Presumably the previous failure of such well known lipophilic, Na+ complexing molecules as antamanide, perhydroan-tamanide, or Lehn s cryptates to render bilayers selectively permeable to Na+ is due to kinetic limitations on their rate of complexation and decomplexation). 

Figure 8.4. Dimyristovl phosphatidic acid. Isotherm obtained at 23°C on a subphase containing 10 JM NaCI and 5 x 10-5m EDTA. The letters denote the points on the isotherm at which the diffraction peaks shown in Figure 8.5 were obtained. (This figure is reproduced from Helm, C.A., Mohwald, H., Kjaer, K. and Als-Nielsen, J. 1987 Biophys. J. 52 381-90 by kind permission of the Biophysical Society and the authors.)...

T. Hianik, I. Grman and M. Thompson, Book of Abstracts. 2nd Symposium of Slovak Biophysical Society, Herl any, Slovakia, March 26-29, 2006. 

Fig. 21 Proposed mechanisms of lipoplex formation (a) vesicle titration (DNA initially in excess) -DNA coats the vesicle surfaces as the latter are added to the DNA solution - with increase of the vesicle concentration, clusters of DNA-coated vesicles form and consequently rupture (b) DNA titration (lipid initially in excess) - DNA encounters with bare membranes result in vesicle associations - vesicle-DNA-vesicle adhesion generates stresses, which lead to vesicle rupture, followed by continued aggregation and growth of the complex upon further addition of DNA. (reproduced with permission from [67] copyright (2000) Biophysical Society)...

Fig. 23 (a) Small-angle X-ray diffraction profile of EDOPC lipoplexes at 4 1 lipid/DNA weight ratio (arrow points to the peak originating from DNA-DNA in-plane correlation) inset, thin-section electron microscopy image of EDOPC lipoplexes (reproduced with permission from [81] copyright (2007) Elsevier), (b) Electron density profiles of the lipid bilayer in presence and in absence of DNA [16] (copyright (2000) Biophysical Society)... 

Fig. 25 (a) DNA release from EDOPC-DNA lipoplexes after addition of negatively charged lipid dispersion, as monitored by FRET (CM, oleic acid DOPA, dioleoyl phosphatidic acid DOPG, dioleoyl phosphatidylglycerol CL, cardiolipin DOPS, dioleoyl phosphatidylserine PI, phospha-tidylinositol). (b) Fraction of released DNA from EDOPC lipoplexes 10 min after addition of the respective anionic liposomes (c) X-ray diffraction patterns of mixtures of EDOPC and anionic liposome dispersions the respective structures are shown schematically on the left side (reproduced with permission from [98] copyright (2004) Biophysical Society)... 

Bailey, M. A., and Devor, D. C. 2007. Modification of a conserved cysteine residue within S6 alters the calcium activation of hIKl and rSK3. Biophysical Society 95a. 

Adapted from Fig. 7 of ref. 73 with permission from the Biophysical Society). 

Janmey, P.A., Tang, J.X., and Schmidt, C.F. Actin Filaments, In Biophysics Textbook, On-Line (V. Bloomeld, Ed.), Sponsored by the Biophysical Society (1999), http //www.biophysics. org/education/ janmey.pdf. 

V. Adrian Parsegian is chief of the Laboratory of Physical and Structural Biology in the National Institute of Child Health and Human Development. He has served as Editor of the Biophysical Journal and President of the Biophysical Society. He is happiest when graduate students come up to him after a lecture and ask hard questions. 

Fig. 3. (A) Far-field confocal micrograph (35 pm x 35 pm) of a mica-supported DPPC monolayer showing LE-LC phase coexistence, deposited at a surface pressure of 9mN/m. (B) Atomic force micrograph of the film depicted in (A). Bright features denote topographically higher substructure of the film. (C) Near-held fluorescence image of the him shown in (A). (D) Near-held topology image collected simultaneously with the image depicted in (C). Reproduced with permission from Ref. [18]. Copyright 1998 Biophysical Society.

Fig. 8. An AFM image of a DPPC bilayer formed using a combination of the LB and LS film transfer techniques. Three distinct height levels are seen that correspond to the layering of LE on LE, LE on LC (or LC on LE), and LC on LC. Reproduced with permission from Ref. [18]. Copyright 1998 The Biophysical Society.

Fig. 10. (Top) Schematic of the experimental arrangement for carrying out NSOM/ FRET measurements. An acceptor dye of a FRET pair is attached to the NSOM probe while the sample contains the donor dye in the bottom and top layers of a multi-layer film. The left fluorescence image shows the donor fluorescence and the right the fluorescence from the tip-bound acceptor dye. Reproduced with permission from Ref. [26]. Copyright 1999 The Biophysical Society.

Fig. 5. IR external reflection absorption spectra of a 7 1 DPPC-d62 DPPG+ 5 wt.% SP-B/C monolayer film collected at surface pressures from 6 to 60mN/m. (A) CH2 stretching region between 3000 and 2800 cm-1. (B) CD2 stretching region between 2250 and 2050 cm-1. Taken from Ref. [65] with permission from Biophysical Society.

Fig. 9. (A) Surface pressure vs. area per amino acid residue of a KLAL film spread from an aqueous buffer solution. (B) IRRAS spectra of the KLAL film during the compression at the respective areas per amino acid residues at positions a-f of the surface pressure area curve in (A). The intensity of the spectra taken at positions e and f has been reduced by a factor of 2 for clarity. All spectra have been recorded at an angle of incidence of 40° and with p-polarized light. Taken from Ref. [72] with permission from Biophysical Society.

Fig. 12. Scheme of the PM-IRRAS setup at the air-water interface. Taken from Ref. [90] with permission from Biophysical Society. 

Author would like to than European Biochemical Society, American Association for the Advancement of Science, Biophysical Society, Elsevier, Current Opinion in Structural Biology, National Academy of Sciences USA for permission to reproduce Figures. VR is supported by grants from NSF. 

Biophysical Society Bench>Press http //submit.biophysj.org/ ctst=y... 

Kropf, A. (1975) in Abstracts of Annual Meeting of Biophysical Society of Japan, p. 281. 

Figure 19 Time-dependent fluorescent monitoring of free Mg + in neuroblastomas cells demonstrates the Li+/Mg + competition that releases bormd Mg + (curve B) Li-perfused cells, compared to rmtreated cells (curve A). Each frame represents 0.33 seconds. (Ref. 124. Reproduced by permission of Biophysical Society)...

Schwille P, Haustein E. Ruorescence correlation spectroscopy. Biophysical Society, http //www.biophysics.org/education/schwille.pdf. Valeur B, Editor. Molecular Ruorescence Principles and Apphcations. 

Figure 4 The modified stalk mechanism of membrane fusion and inverted phase formation, (a) planar lamellar (La) phase bilayers (b) the stalk intermediate the stalk is cylindrically-symmetrical about the dashed vertical axis (c) the TMC (trans monolayer contact) or hemifusion structure the TMC can rupture to form a fusion pore, referred to as interlamellar attachment, ILA (d) (e) If ILAs accumulate in large numbers, they can rearrange to form Qn phases, (f) For systems close to the La/H phase boundary, TMCs can also aggregate to form H precursors and assemble Into H domains. The balance between Qn and H phase formation Is dictated by the value of the Gaussian curvature elastic modulus of the bIlayer (reproduced from (25) with permission of the Biophysical Society) The stalk in (b) is structural unit of the rhombohedral phase (b ) electron density distribution for the stalk fragment of the rhombohedral phase, along with a cartoon of a stalk with two lipid monolayers merged to form a hourglass structure (reproduced from (26) with permission of the Biophysical Society).

Source Claser, R. W., Sachse, C., Durr, U. H. N. etal., Concentration-dependent realignment of the antimicrobial peptide PCLa in lipid membranes observed by solid-state F-19-NMR, Biophys. /. (2005) 88, 3392-3397. Reproduced with permission from the Biophysical Society.)... 

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