THE IMPORTANCE OF THE PRACTICE OF COMPETITIVE GAMES KID’S ATHLETICS IN PHYSICAL EDUCATION FOR COLLEGE STUDENTS (11-12 YEARS) USING THE COOPERATIVE LEARNING STRATEGY

Physical education teachers should purposefully accept the fact that they are the role models in developing individual and group characteristics. In addition, teachers should structure competitive activities to maximize the participation of all students. In this regard, teaching physical education is an exciting experience. It is important that we teach more than just knowledge, skills, and strategies like cooperative strategy and other. From this perspective, the teacher must model the desired outcome in the same way he demonstrates the critical elements of a kids' athletics. The aim of this experimental study is to determine the effect of the practice of the cooperation strategy with a new concept of Kids' Athletics; their contribution towards the improvement of teaching conditions in lessons of Physical Education and Sports in middle School; and the improvement of sports performance among students of the middle School in long jump (m), shot put (m), sprint 50 m (s), and endurance racing 1000 m (s). Thus, this study is one of the very best practices that promote a higher level of participation among all students in physical education. It is designed to give children the pleasure of playing athletics. It helps them to embark on sprinting, endurance running, jumping, and throwing. Two groups of girls (aged 11 ± 0.65 years) participated in this study. The students were divided into experimental and control group (n=24). The results according to the research variables is characterized by significant differences (*p≤0.05). Consequently, teacher’s use of the cooperative learning techniques in physical education will encourage a higher level of participation among many students in the activities of the kids' athletics. Therefore, this will improve the physical performance of students and their relationships better than the traditional teaching method using a command style (Mosston & Ashworth, 2002)

Thermotropic and structural effects of poly(malic acid) on fully hydrated multilamellar DPPC–water systems

The thermotropic and structural effects of low molecular weight poly(malic acid) (PMLA) on fully hydrated multilamellar dipalmitoylphosphatidylcholine (DPPC)-water systems were investigated using differential scanning calorimetry (DSC), small-angle X-ray scattering (SAXS), and freeze-fracture transmission electron microscopy (FFTEM). Systems of 20 wt% DPPC concentration and 1 and 5 wt% PMLA to lipid ratios were studied. The PMLA derivatives changed the thermal behavior of DPPC significantly and caused a drastic loss in correlation between lamellae in the three characteristic thermotropic states (i.e., in the gel, rippled gel and liquid crystalline phases). In the presence of PBS or NaCl, the perturbation was more moderate. The structural behavior on the atomic level was revealed by FTIR spectroscopy. The molecular interactions between DPPC and PMLA were simulated via modeling its measured infrared spectra, and their peculiar spectral features were interpreted. Through this interpretation, the poly(malic acid) is inferred to attach to the headgroups of the phospholipids through hydrogen bonds between the free hydroxil groups of PMLA and the phosphodiester groups of DPPC

Characterization of the Interactions between Fluoroquinolone Antibiotics and Lipids: a Multitechnique Approach

Probing drug/lipid interactions at the molecular level represents an important challenge in pharmaceutical research and membrane biophysics. Previous studies showed differences in accumulation and intracellular activity between two fluoroquinolones, ciprofloxacin and moxifloxacin, that may actually result from their differential susceptibility to efflux by the ciprofloxacin transporter. In view of the critical role of lipids for the drug cellular uptake and differences observed for the two closely related fluoroquinolones, we investigated the interactions of these two antibiotics with lipids, using an array of complementary techniques. Moxifloxacin induced, to a greater extent than ciprofloxacin, an erosion of the DPPC domains in the DOPC fluid phase (atomic force microscopy) and a shift of the surface pressure-area isotherms of DOPC/DPPC/fluoroquinolone monolayer toward lower area per molecule (Langmuir studies). These effects are related to a lower propensity of moxifloxacin to be released from lipid to aqueous phase (determined by phase transfer studies and conformational analysis) and a marked decrease of all-trans conformation of acyl-lipid chains of DPPC (determined by ATR-FTIR) without increase of lipid disorder and change in the tilt between the normal and the germanium surface (also determined by ATR-FTIR). All together, differences of ciprofloxacin as compared to moxifloxacin in their interactions with lipids could explain differences in their cellular accumulation and susceptibility to efflux transporters

Kinetic analysis of the nucleic acid chaperone activity of the Hepatitis C virus core protein

The multifunctional HCV core protein consists of a hydrophilic RNA interacting D1 domain and a hydrophobic D2 domain interacting with membranes and lipid droplets. The core D1 domain was found to possess nucleic acid annealing and strand transfer properties. To further understand these chaperone properties, we investigated how the D1 domain and two peptides encompassing the D1 basic clusters chaperoned the annealing of complementary canonical nucleic acids that correspond to the DNA sequences of the HIV-1 transactivation response element TAR and its complementary cTAR. The core peptides were found to augment cTAR-dTAR annealing kinetics by at least three orders of magnitude. The annealing rate was not affected by modifications of the dTAR loop but was strongly reduced by stabilization of the cTAR stem ends, suggesting that the core-directed annealing reaction is initiated through the terminal bases of cTAR and dTAR. Two kinetic pathways were identified with a fast pre-equilibrium intermediate that then slowly converts into the final extended duplex. The fast and slow pathways differed by the number of base pairs, which should be melted to nucleate the intermediates. The three peptides operate similarly, confirming that the core chaperone properties are mostly supported by its basic clusters

Interactions between fluoroquinolones and lipids : biophysical studies

Probing fluoroquinolones/lipid interactions at the molecular level represents an important challenge in both membrane biophysics and pharmaceutical research. As the pharmacological target of these antibiotics is intracellular, they must pass across the bacterial membranes. Likewise, fluoroquinolones enter eukaryotic cells, which imply their ability of interacting with lipids membranes. In this context, the aim of my Thesis has been to characterize the effect of two closely related fluoroquinolones, ciprofloxacin and moxifloxacin, on physicochemical properties of the major phospholipids DPPG and DOPC/DPPC that are mimicking the prokaryotic and eukaryotic lipid membranes, respectively, by means of biophysical methods. First, I have studied the effect of these drugs on domains lipids erosion, lipids packing and their ability of modifying the conformation and orientation of the acyl chain(s) of phospholipids. Second, I have determined the binding affinities of ciprofloxacin to different model lipid membranes (DPPG, DPPC) and its effects on head group mobility and on thermotropic profile of these two phospholipids. The data reported in this Thesis point to different effects of ciprofloxacin and moxifloxacin on the phospholipids tested. Indeed, moxifloxacin induces more changes in the acyl chain conformation of phospholipids and has more lipid packing effects than ciprofloxacin. The latter interacts primarily with the head groups of lipids, and thereby modifies the orientation of the acyl chain. Thus, the first step in the interaction of ciprofloxacin with lipid membranes relates to its binding to these headgroups, which is stronger with negatively charged (DPPG) than with zwitterionic phospholipids (DPPC). Conversely, our results suggest that moxifloxacin is located in a more hydrophobic environment of the membranes, probably by creating a pocket in the interior of the lipid bilayer. These contrasting behaviors may be related to the fact that ciprofloxacin is, globally speaking, a more hydrophilic drug than moxifloxacin. Our work may help in shedding more light on the role played by lipids in the transport of fluoroquinolones in both prokaryotic and eukaryotic cells.(FARM 3) -- UCL, 201

Image restoration using a reaction-diffusion process

This study shows how partial differential equations can be employed to restore a digital image. It is in fact a generalization of the work presented by Catte [12], which modify the Perona-Malik Model by nonlinear diffusion. We give a demonstration of the consistency of the reaction-diffusion model proposed in our work

Kinetic analysis of the nucleic acid chaperone activity of the Hepatitis C virus core protein

10.1093/nar/gkq094NUCLEIC ACIDS RESEARCH38113632-364

Interactions Of Ciprofloxacin With Dppc And Dppg: Fluorescence Anisotropy, Atr-Ftir And P-31 Nmr Spectroscopies And Conformational Analysis

The interactions between a drug and lipids may be critical for the pharmacological activity. We previously showed that the ability of a fluoroquinolone antibiotic, ciprofloxacin, to induce disorder and modify the orientation of the acyl chains is related to its propensity to be expelled from a monolayer upon compression [1]. Here, we compared the binding of ciprofloxacin on DPPC and DPPG liposomes (or mixtures of phospholipids [DOPC:DPPC], and [DOPC:DPPG]) using quasi-elastic light scattering and steady-state fluorescence anisotropy. We also investigated ciprofloxacin effects on the transition temperature (T(m)) of lipids and on the mobility of phosphate head groups using Attenuated Total Reflection Fourier Transform Infrared-Red Spectroscopy (ATR-FTIR) and (31)P Nuclear Magnetic Resonance (NMR) respectively. In the presence of ciprofloxacin we observed a dose-dependent increase of the size of the DPPG liposomes whereas no effect was evidenced for DPPC liposomes. The binding constants K(app) were in the order of 10(5) M(-1) and the affinity appeared dependent on the negative charge of liposomes: DPPG>DOPC:DPPG (1:1; M:M)>DPPC>DOPC:DPPC (1:1; M:M). As compared to the control samples, the chemical shift anisotropy (Deltasigma) values determined by (31)P NMR showed an increase of 5 and 9 ppm for DPPC:CIP (1:1; M:M) and DPPG:CIP (1:1; M:M) respectively. ATR-FTIR experiments showed that ciprofloxacin had no effect on the T(m) of DPPC but increased the order of the acyl chains both below and above this temperature. In contrast, with DPPG, ciprofloxacin induced a marked broadening effect on the transition with a decrease of the acyl chain order below its T(m) and an increase above this temperature. Altogether with the results from the conformational analysis, these data demonstrated that the interactions of ciprofloxacin with lipids depend markedly on the nature of their phosphate head groups and that ciprofloxacin interacts preferentially with anionic lipid compounds, like phosphatidylglycerol, present at a high content in these membranes