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PubMed1992

Temperature dependence and Arrhenius activation energy of F-actin velocity generated in vitro by skeletal myosin.

The effect of temperature on the velocity of rhodamine phalloidin-labelled F-actin moving in vitro on rabbit skeletal myosin has been studied. Translating actin filaments were visualized by epi-fluorescence in an inverted microscope, equipped with temperature control (+/- 0.2 K) of the stage and objective. Images were recorded in real time at magnifications of 400x or 160x by an intensified CCD camera on video tape. Motion of individual filaments was tracked by hand and velocities determined using frame times recorded simultaneously on the video tape. Velocity changed from 12 microns per second at 42 degrees C to 11 nm per second at 3 degrees C. The Arrhenius plot is non-linear, with the data following a cubic regression curve with no evident breaks or jumps. Data taken over the temperature range from single preparations followed the same curve for both heating and cooling; this indicates reversibility and absence of hysteresis. A hyperbolic model that smoothly translates with temperature between two asymptotic activation energies fits the data above 7 degrees C: these energies are 50(+/- 5) kJ per mole (Q10 = 1.9) at high temperatures and 289(+/- 29) kJ per mole (Q10 = 76.5) at low temperature with a transition temperature of 15.4(+/- 0.6) degrees C. These values are compared with other measurements made in vitro, in solution studies and on muscle fibres. An Arrhenius activation energy of 50 kJ per mole and a transition temperature of 15 degrees C are consistent with previous determinations but 289 kJ per mole is significantly greater than has been seen at low temperatures in other systems. This may indicate a different rate-limiting step in the kinetics of skeletal myosin driving actin filaments in vitro below 15 degrees C. Current determinations of the myosin "step-size" assume that the actin velocity is determined by the rate of ATP hydrolysis; the data confirm similar activation energies above 20 degrees C but they show that the temperature dependencies and activation energies are different at lower temperatures, implying uncoupling of the two processes.

Actins↗
PubMed1977

Exchange and aggregation in dispersions of dimyristoyl phosphatidylcholine vesicles containing myristic acid.

Processes occurring in dispersions of dimyristoyl phosphatidylcholine containing myristic acid have been studied by light scattering of dilute dispersions (concn. less than or equal to 1 mg/ml) at temperatures above and below the phase transition temperatures of these dispersions. The transition temperatures increase with increasing mol fraction of myristic acid. Above these temperatures, vesicles with different mol fractions of myristic acid exchange lipid molecules. The exchange process leads to vesicles having phase transition temperatures and radii, which ar both intermediate between the initial transitions and radii, respectively. In contrast with the observations above the phase transitions, it was found that when dimyristoyl phosphatidylcholine/myristic acid vesicles were cooled to a few degrees below the phase transition, larger particles were formed. These observations are consistent with a mechanism consisting of vesicle aggregation followed by fustion of the aggregated vesicles. The aggregation process is of second order in the vesicle concentration, and its rate increases with increasing mol fraction of myristic acid.

Kinetics↗
PubMed1992

Hydrophobicity of amino acid residues: differential scanning calorimetry and synthesis of the aromatic analogues of the polypentapeptide of elastin.

Relative hydrophobicities of aromatic amino acid residues are investigated by using differential scanning calorimetry (DSC) on 10 synthetic copolypentapeptides of poly(VPGVG) of elastin. Utilizing the hydrophobic-driven process of the inverse temperature transition exhibited by these polypentapeptides in aqueous solution, the relative hydrophobicities of Phe, Trp, and Tyr residues are determined by the critical temperature and heat of the transition. The DSC data for the aromatic residue containing copolypentapeptide aqueous solution indicate that tryptophan is the most hydrophobic amino acid residue, phenylalanine the third most hydrophobic on basis of transition temperature and the second on basis of transition heat. For tyrosine, significant differences are observed between the phenolic and the phenoxide anionic states. At pH 7, where tyrosine is protonated, it is found to be the second most hydrophobic amino acid residue on the basis of the transition temperature, whereas on the basis of the heat of transition, it is less hydrophobic than both tryptophan and phenylalanine. Changing the pH from pH 7 to pH 12, for example, for poly[0.8(VPGVG), 0.2(VPGYG)] in aqueous solution shifts the transition temperature from 7 to 49 degrees C with a dramatically reduced heat. On the basis of both the transition temperature scale and the heat of transition, the hydroxylated tyrosine appears less hydrophobic than glycine.

Amino Acid Sequence↗
PubMed1981

Interactions of dipalmitoyl- and dimyristoylphosphatidylcholines and their mixtures with apolipoprotein A-I.

Human and bovine A-I apolipoproteins were incubated with multibilayer liposomes of dimyristoylphosphatidylcholine (DMPC) and dipalmitoylphosphatidylcholine (DPPC) and several mixtures of these two lipids. The reactions were carried out at temperatures around the transition temperature of the lipids, and the formation of small, micellar complexes of protein with lipid was followed as a function of time. Micellar complexes were isolated by ultracentrifugation and were characterized in terms of stoichiometry, lipid composition by gas chromatography, approximate size by gel filtration, and phase transition behavior by fluorescence polarization measurements. The results indicate a decrease in reaction rates with increasing DPPC contents of the mixtures, consistent with the higher stability of DPPC bilayers. Reactions have optimal rates at the transition temperature and are limited to the temperature range where gel and liquid-crystalline phases coexist. The isolated complexes with DMPC and DPPC have similar molecular weights in the range from 2 X 10(5) to 2.5 X 10(5), but lipid/protein mole ratios differ by about 40%. The lower lipid/protein ratio of DPPC complexes (100:1 mol/mol) is compensated by the longer acyl chains of this lipid, such that the acyl chain area of both complexes stabilized by apolipoprotein is essentially identical.

Animals↗
PubMed1977

Polymeric debris in synovium after total joint replacement: histogical identification.

In studying a series of synovial biopsy specimens from patients with loose joint replacements, we were able to differentiate reliably between polymethylmethacrylate and ultra high-molecular-weight polyethylene by observing alterations in their birefringence with changes in temperature. The glass transition temperature of polymethylmethacrylate (when it softens from a glass-like to a rubber-like state) is about 105 degrees centigrade. Polyethylene melts at 135 degrees centigrade. The birefringence in polyethylene returns after it has been melted and then cooled; this is not true of methylmethacrylate fragments heated above their glass transition temperature. When cooled, methacrylate fails to regain its birefringence. In addition, free particles of the two plastics were studied in vitro to validate this method of differentiation. We recommend its use routinely in histological studies of patients with loosening.

Arthroplasty↗
PubMed1980

Lateral diffusion of M-13 coat protein in mixtures of phosphatidylcholine and cholesterol.

The translational diffusion of fluorescent-labeled M-13 phage coat protein (FITC-M-13), an integral membrane protein, has been measured in mixtures of phosphatidylcholines and cholesterol, using a pattern photobleaching technique. At temperatures below the chain-melting transition temperature of dimyristoylphosphatidylcholine (DMPC) (23.8 degrees C), the lateral diffusion coefficient of M-13 shows a marked increase when the cholesterol concentration is increased above 20 mol %. A similar marked increase in the lateral diffusion coefficient of a fluorescent phospholipid is also observed. At temperatures above the chain-melting transition temperature of DMPC, a minimum is observed in the lateral diffusion coefficient of FITC-M-13 for cholesterol concentrations in the vicinity of 25 mol %. This minimum in the diffusion coefficient of FITC-M-13 is also observed at 25 mol % cholesterol in egg phosphatidylcholine at 15 degrees C. No such minimum is observed for the lateral diffusion coefficient of the fluorescent lipid. The lateral diffusion coefficient of FITC-M-13 is large (greater than 10(-9) cm2/s) at all cholesterol concentrations for temperatures above the chain-melting transition temperature of the phosphatidylcholine. Several other proteins contain hydrophobic regions similar to that of the M-13 coat protein. We anticipate that a number of proteins of this type will show similar diffusional behavior, in particular exhibiting rapid diffusion throughout a wide range of lipid composition.

Cholesterol↗
PubMed2004

The complex kinetics of protein folding in wide temperature ranges.

The complex protein folding kinetics in wide temperature ranges is studied through diffusive dynamics on the underlying energy landscape. The well-known kinetic chevron rollover behavior is recovered from the mean first passage time, with the U-shape dependence on temperature. The fastest folding temperature T0 is found to be smaller than the folding transition temperature Tf. We found that the fluctuations of the kinetics through the distribution of first passage time show rather universal behavior, from high-temperature exponential Poissonian kinetics to the relatively low-temperature highly non-exponential kinetics. The transition temperature is at Tk and T0 < Tk < Tf. In certain low-temperature regimes, a power law behavior at long time emerges. At very low temperatures (lower than trapping transition temperature T < T0/(4 approximately 6)), the kinetics is an exponential Poissonian process again.

Computer Simulation↗
PubMed1997

Synthesis, characterization, biodegradation, and drug delivery application of biodegradable lactic/glycolic acid oligomers: I. Synthesis and characterization.

A series of oligomers or low molecular weight polymers of lactic and/or glycolic acid has been synthesized with different molar ratios of lactic to glycolic acid. These oligomers have been characterized with respect to oligomer composition, molecular weight, intrinsic viscosity, crystallinity, melting temperature, and glass transition temperature. The polymerization conditions for the lactic/glycolic acid oligomer syntheses were as follows: 180-220 degrees C, 5 mm Hg, 5 h, and 0.1 wt% of catalyst (antimony oxide) concentration. The polymeric compositions correlated to the feed ratios of lactic to glycolic acid. The molecular weight of the oligomers ranged from 895.8 +/- 48.7 to 1368.0 +/- 0 D with the intrinsic viscosity ranging from 0.0513 to 0.0814 dl g-1. The lactic/glycolic acid oligomers were found to be amorphous. The glass transition temperatures of the lactic/glycolic acid oligomers were lower than physiological temperature.

Biodegradation, Environmental↗
PubMed1984

Effect of temperature on transition and transversion mutagenesis: characterization of wild type and a mutator T4 DNA polymerase mutant.

The effect of temperature on genetically well-defined mutational pathways was examined in the bacteriophage T4. The mutational site was a T4 rII ochre mutant which could revert to rII+ via a transversion or to the amber convertant via a transition. Temperature did not strongly affect any of the pathways examined in a wild-type background; however, increased temperature reduced the mutational activity of a mutator DNA polymerase mutant. Possible models to explain the role of temperature in mutagenesis are discussed as well as the significance of low temperatures for in vitro mutagenesis reactions.

DNA-Directed DNA Polymerase↗
PubMed1991

Effect of insulin on the lytic action of lysophosphatidylcholine in lipid bilayers.

The effect of insulin on the bilayer properties of dimyristoylphosphatidylcholine liposomes at the gel and the liquid crystalline state was measured by differential scanning calorimetry and absorbance at 450 nm. It is found that insulin promotes a decrease in the enthalpy of the gel-liquid crystalline transition without displacing the transition temperature. Under these conditions the lytic action of monomyristoylphospatidylcholine is enhanced, decreasing the critical lytic concentrations to values comparable to the bilayer at the gel state. The effect of the lysoderivate on liposomes in contact with increasing concentrations of insulin promotes a reorganization of the lipids into smaller particles as inferred from fluorescence dequenching, turbidity and exclusion chromatography assay. It is concluded that the action of lysoderivates can be enhanced, at temperatures above the transition temperature, by proteins that without spanning the lipid bilayers can perturb the bilayer interface.

Calorimetry, Differential Scanning↗
PubMed1993

Thermodynamic stability and osmotic sensitivity of small unilamellar phosphatidylcholine vesicles.

Evidence is presented to show that small unilamellar phosphatidylcholine vesicles with a diameter of approx. 20 nm are osmotically sensitive. Such vesicles respond to osmotic pressure by swelling or shrinking depending on the direction of the applied salt gradient. This is true for small unilamellar vesicles of egg phosphatidylcholine and dimyristoylphosphatidylcholine below and above their crystal-to-liquid crystal transition temperature. At the transition temperature the vesicles are osmotically insensitive due to the increased bilayer permeability resulting in rapid dissipation of salt gradients. Positive salt gradients produce shrinking and collapse of spherical phospholipid vesicles to disks. Shrinking of vesicles is associated with H2O and solute efflux, but only limited solute influx. Clustering of lipid molecules in the bilayers of the resulting disks can be detected by EPR spin labeling. Negative salt gradients produce swelling of vesicles which is associated with H2O and solute influx. Our experiments are consistent with an osmotically perturbed bilayer. In the presence of osmotic gradients the influx and efflux of H2O is coupled with the movement of ions and small molecules which in the absence of salt gradients or osmotic stress cannot pass the phospholipid bilayer. However, during osmotically induced shrinking and swelling of SUV the integrity of the phospholipid bilayer is maintained to the extent that vesicles do not break, and therefore equilibration between external medium and vesicle cavity does not take place.

Dimyristoylphosphatidylcholine↗
PubMed1999

Influence of plasticizers and drugs on the physical-mechanical properties of hydroxypropylcellulose films prepared by hot melt extrusion.

Hydroxypropylcellulose (HPC) films containing drugs or hydrophilic or hydrophobic plasticizers were prepared by a hot melt extrusion process. Polyethylene glycol 8000 (PEG 8000) 2%, triethyl citrate (TEC) 2%, acetyltributyl citrate (ATBC) 2%, and polyethylene glycol 400 (PEG 400) 1% were the plasticizing agents studied. In addition, either hydrocortisone (HC) 1% or chlorpheniramine maleate (CPM) 1% was incorporated into the films as a model drug. The physical-mechanical properties of the films that were investigated included tensile strength (TS), percentage elongation (%E), and Young's modulus (YM). Differential scanning calorimetry (DSC) was utilized to determine glass transition temperatures (Tg's). These parameters were studied as a function of time and temperature. The glass transition temperatures initially decreased with the inclusion of the drugs and plasticizers. However, after 6 months aging, films containing PEG 400 and HC showed a marked increase in Tg. The films containing PEG 400 showed physical-mechanical instability in all parameters studied. All extruded films exhibited a marked decrease in TS in contrast to a large increase in %E when testing was performed perpendicular to flow versus in the direction of flow. In addition, a consistent film of HPC in the absence of drugs or plasticizers could not be extruded due to the excessive stress on the equipment. Although the theoretical percentage of CPM on aging remained fairly constant over the processing temperature ranges in this study, the HC levels remaining in the extruded films during storage were a function of time and temperature.

Cellulose↗
PubMed2006

Slow dynamics of shape recovery of disordered nematic elastomers.

A loosely cross-linked liquid crystal elastomer (LCE) having a disordered director alignment (polydomain texture) slowly recovers to their original shape from the deformed state in the order of 10(3) s after the imposed field is removed. The mesogen alignment at the cross-linking stage greatly affects the shape recovery dynamics of polydomain LCEs, whereas it has no appreciable influence on the equilibrium characteristics such as the nematic-isotropic transition temperature, degree of swelling, and field-induced strain. The shape recovery of a LCE formed in the polydomain nematic state is considerably faster than that originally prepared in the isotropic state because of the memory effect of the initial director distribution at the cross-linking stage. The relaxation time rapidly increases as the temperature approaches the transition temperatures; this is independent of the initial mesogen alignment during cross linking.

Journal Article↗
PubMed2002

Compressibility divergence and the finite temperature Mott transition.

In the context of the dynamical mean-field theory (DMFT) of the Hubbard model, we study the behavior of the compressibility near the density driven Mott transition at finite temperatures. We demonstrate this divergence using DMFT and quantum Monte Carlo simulations in the one-band and the two-band Hubbard model. We supplement this result with considerations based on the Landau theory framework, and discuss the relevance of our results to the alpha-gamma end point in cerium.

Journal Article↗
PubMed1981

Titration of the phase transition of phosphatidylserine bilayer membranes. Effects of pH, surface electrostatics, ion binding, and head-group hydration.

The dependence of the gel-to-fluid phase transition temperature of dimyristoyl- and dipalmitoylphosphatidylserine bilayers on pH, NaCl concentration, and degree of hydration has been studied with differential scanning calorimetry and with spin-labels. On protonation of the carboxyl group (pK2app = 5.5), the transition temperature increases from 36 to 44 degrees C in the fully hydrated state of dimyristoylphosphatidylserine (from 54 to 62 degrees C for dipalmitoylphosphatidylserine), at ionic strength J = 0.1. In addition, at least two less hydrated states, differing progressively by 1 H2O/PS, are observed at low pH with transition temperatures of 48 and 52 degrees C for dimyristoyl- and 65 and 68.5 degrees C for dipalmitoylphosphatidylserine. On deprotonation of the amino group (pK3app = 11.55) the transition temperature decreases to approximately 15 degrees C for dimyristoyl- and 32 degrees C for dipalmitoylphosphatidylserine, and a pretransition is observed at approximately 6 degrees C (dimyristoylphosphatidylserine) and 21.5 degrees C (dipalmitoylphosphatidylserine), at J = 0.1. No titration of the transition is observed for the fully hydrated phosphate group down to pH less than or equal to 0.5, but it affinity for water binding decreases steeply at pH greater than or equal to 2.6. Increasing the NaCl concentration from 0.1 to 2.0 M increases the transition temperature of dimyristoyphosphatidylserine by approximately 8 degrees C at pH 7, by approximately 5 degrees at pH 13, and by approximately 0 degrees C at pH 1. These increases are attributed to the screening of the electrostatic titration-induced shifts in transition temperature. On a further increase of the NaCl concentration to 5.5 M, the transition temperature increases by an additional 9 degree C at pH 7, 13 degree C at pH 13, approximately 7 degree C in the fully hydrated state at pH 1, and approximately 4 and approximately 0 degree C in the two less hydrated states. These shifts are attributed to displacement of water of hydration by ion binding. From the salt dependence it is deduced that the transition temperature shift at the carboxyl titration can be accounted for completely by the surface charge and change in hydration of approximately 1 H2O/lipid, whereas that of the amino group titration arises mostly from other sources, probably hydrogen bonding. The shifts in pK (delta pK2 = 2.85, delta pK3 = 1.56) are consistent with a reduced polarity in the head-group region, corresponding to an effective dielectric constant epsilon approximately or equal to 30, together with surface potentials of psi congruent to -100 and -150 mV at the carboxyl and amino group pKs, respectively. The transition temperature of dimyristoylphosphatidylserine-water mixtures decreases by approximately 4 degree C each water/lipid molecule added, reaching a limiting value at a water content of approximately 9-10 H2O/lipid molecule.

Calorimetry, Differential Scanning↗
PubMed1981

Hexagonal phases in phospholipids with saturated chains: phosphatidylethanolamines and phosphatidic acids.

The structure of phospholipids with saturated chains was investigated by differential scanning calorimetry and by X-ray diffraction. It is shown that both phosphatidylethanolamines and phosphatidic acids can exhibit a hexagonal phase at high temperature. The temperature of the transition to the hexagonal phase is dependent on chain length and sodium salt concentration. Increasing the chain length or the sodium salt concentration results in a decrease in the transition temperature. In addition to this transition at high temperature, a calorimetric transition at low temperature, a calorimetric transition at low temperature is detected in some phospholipids.

Calorimetry, Differential Scanning↗
PubMed1981

Interaction of alpha-lactalbumin with dimyristoyl phosphatidylcholine vesicles. II. A fluorescence polarization study.

The interaction of alpha-lactalbumin with dimyristoyl phosphatidylcholine vesicles was studied as a function of temperature, pH and the molar ratio of phospholipid to protein. The method consisted of measuring the fluorescence polarization of 1,6-diphenyl-1,3,5-hexatriene used as a probe embedded in the vesicles. After incubation of the protein with the phospholipid for 2 h at 23 degrees C, the polarization of the light emitted by this probe shifted to higher values; the shift was greater at acidic pH than at neutral pH. After incubation at 37 degrees C, no shift in polarization was found at pH 7, 6 and 5 while a strong increase occurred at pH 4. Lowering the temperature, after incubation at 37 degrees C, had little effect on the polarization at neutral pH. At pH 5, however, and in the transition range of the phospholipid, the polarization increased greatly. A kinetic study of the interaction carried out around the transition temperature of dimyristoyl phosphatidylcholine as a function of pH shows that the speed of complex formation between alpha-lactalbumin and the lipid increases from neutral to acidic pH. From the present results and in agreement with our earlier calorimetric and fluorescence data (Hanssens, I., Houthuys, C., Herreman, W. and van Cauwelaert, F.H. (1980) Biochim. Biophys, Acta 602, 539--557), it is concluded that at neutral pH the interaction mechanism is probably different from that at acidic pH. At neutral pH and at all temperatures, alpha-lactalbumin is mainly absorbed electrostatically to the outer surface of the vesicle with little or no influence on the transition temperature of the phospholipid. At this pH, only around the transition temperature is penetration possible. At pH 4, however, the protein is able to penetrate the vesicle at all temperatures and to interact hydrophobically with the phospholipid fatty acid chains. As a result of this interaction, the transition temperature is increased by about 4 degrees C. This different behaviour changes progressively upon acidification: at pH 5, penetration seems to be impossible at temperatures far above the transition temperature but occurs rapidly around the transition temperature.

Animals↗
PubMed1991

Thermorheologic properties of aqueous solutions and gels of Tetronic 1508.

The rheologic properties of aqueous solutions and gels of Tetronic 1508 were investigated as a function of polymer concentration and temperature utilizing rotational viscometry. Below the sol-gel transition temperature the polymer solutions were low in viscosity and exhibited Newtonian rheologic behavior even at concentrations of 20 and 25% (w/w). Upon sol-gel transition, the more concentrated polymer solutions underwent a dramatic four- to five-orders of magnitude increase in viscosity, resulting in the formation of a rigid gel structure. Above the sol-gel transition temperature, the gels displayed pseudoplastic and plastic rheologic properties and the viscosity of the gels remained at a relatively constant value over a wide temperature range. Eventually, the thermal energy of the system exceeded the bonding forces within the gel structure, resulting in a gel-sol transition which was marked by a dramatic decrease in the viscosity of the system. Above the gel-sol transition temperature, the system reverted to a Newtonian fluid with viscosities very similar to those found for the Tetronic 1508 solutions at temperatures below the sol-gel transition temperature. The thermodynamic implications of the gel-sol transition are discussed.

Chemical Phenomena↗