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The purpose of this study was to find the factors responsible for winning in the men’s and women’s beach volleyball championship. Materials and methods. The study sample consisted of a total of 212 matches for men and 214 matches for women of the 2017 & 2019 FIVB Men and Women Beach Volleyball World Championships held at Vienna & Hamburg from 28 July to 6 Aug 2017 and 28 June to 7 July 2019. The matches were played by 192 teams (both men and women combined) consisting of 384 numbers (both men and women combined) of players from different nations. The data were analyzed using Binary Logistic Regression (Forward: LR Method) with the result of the game as the dependent variable and predictor variables as covariates. β, standard error β, Wald’s χ2, odds ratio with 95% confidence interval were calculated. Model evaluation was conducted using the likelihood ratio test, Cox & Snell (R2), and Nagelkerke (R2) tests. The goodness of fit test for the models was conducted using the Hosmer & Lemeshow test. Results. The analysis revealed seven factors related to winning in men’s and women’s competition. While in league rounds, six factors in men’s and seven factors in women’s competition were related to winning. Besides, in knockout rounds, four factors in men’s and six factors in women’s competition were related to winning. Conclusion. The study shows that there is a significant association of important factors with respect to winning a match in an elite beach volleyball championship. The coaches and players can take note of the important factors responsible for winning in the elite beach volleyball championship, with different factors playing an important role in men’s and women’s competition during league and knockout rounds as well.

Many transcription factors control gene expression by binding to specific DNA sequences at or near the genes that they regulate. However, some transcription factors play more global roles in the control of gene expression by altering the architecture of sections of chromatin or even the whole genome. The ability to form oligomeric protein assemblies allows many of these proteins to manipulate extensive segments of DNA or chromatin via the formation of structures such as DNA loops or protein-DNA fibres.Here we show that the proline rich homeodomain protein PRH/Hhex forms predominantly octameric and/or hexadecameric species in solution as well as larger assemblies. We show that these assemblies are highly stable resisting denaturation by temperature and chemical denaturants.These data indicate that PRH is functionally and structurally related to the Lrp/AsnC family of proteins, a group of proteins that are known to act globally to control gene expression in bacteria and archaea.

PURPOSE: Presently available hepatitis B vaccine is administered through parenteral route and fails to induce mucosal antibody response. Oral immunization appears to be an effective and attractive alternative to the parenteral immunization. However, the problem of degradation of antigen in harsh and hostile environment of the gastrointestinal tract consequently requires larger dose and more frequent dosing of antigen. Furthermore, much larger dose can induce systemic tolerance. In order to overcome these problems bile salt stabilized vesicles (bilosomes) can be used, which could provide both protection to antigen as well as transmucosal uptake and subsequent resultant systemic immunity. Another purpose of this study was to determine the dose that could produce comparable serum antibody titre against hepatitis B through oral route as obtained after intramuscular immunization. METHODS: In the present study bilosomes containing recombinant hepatitis B surface antigen were prepared by cast film method. HBsAg loaded bilosomes were characterized in vitro for their shape, size, percent entrapment and stability. The fluorescence microscopy was carried out to confirm the uptake of bilosomes by gut associated lymphoid tissues (GALT). The in vivo study was comprised of estimation of anti-HBsAg IgG response in serum and anti-HBsAg sIgA in various body secretions using specific ELISA techniques following oral immunization with low dose loaded bilosomes (BSSV1, 10 µg), intermediate dose loaded bilosomes (BSSV2, 20 µg) and high dose loaded bilosomes (BSSV3, 50 µg) in Balb/c mice. RESULTS: The fluorescence microscopy suggests that an increase in fluorescence intensity following the uptake of bilosomes entrapped FITC-BSA in gut associated lymphoid tissues. The high dose HBsAg bilosomes (BSSV3, 50 µg) produced comparable anti-HBsAg IgG levels in serum to those observed in the case of intramuscular administration of alum adsorbed HBsAg (10 µg). However, alum adsorbed HBsAg was unable to produce sIgA in mucosal secretions, whilst, all bilosomal preparations could elicit measurable sIgA in mucosal secretions, where the highest responses were observed in high dose HBsAg bilosomes (BSSV3, 50µg). CONCLUSIONS: HBsAg loaded bilosomes produced both systemic as well as mucosal antibody responses upon oral administration. Thus bilosomes may emerge out to be potential carriers for non invasive mucosal immunization.

The protein-folding catalyst SlyD, a peptidyl prolyl cis – trans isomerase regulated by metal binding, was initially discovered as a major contaminant of non-denaturing immobilized metal-affinity chromatography (IMAC)-based procedures for the purification of heterologously expressed 6×His-tagged proteins from Escherichia coli . Given its ability to bind weakly to nickel-nitrilotriacetic acid (Ni2+-NTA), protocols for the purification of SlyD currently use an initial non-denaturing IMAC step, followed by an ion-exchange chromatographic step and occasionally also other chromatographic steps. Here we demonstrate that using denaturing conditions instead of non-denaturing conditions, and by processing of large quantities of culture through small volumes of Ni2+-NTA resin to increase competition for binding, single-step purification of SlyD to homogeneity can be achieved directly from E. coli extracts, as assessed through spectroscopic and electrophoretic methods. The purified, denatured SlyD is shown to be capable of refolding to give rise to a native-like CD spectrum, establishing the utility of the procedure. The procedure also establishes SlyD to be the only E. coli protein capable of contaminating denaturing IMAC-based procedures. [ABSTRACT FROM AUTHOR]