Forces attributed to dark matter may originate from entangled particles as seen in the shape of galaxies formed by GRBs

Recently, it has been suggested that entangled particles may be connected by a wormhole. If that is right, what is the distance between them we have to take into account when applying Newton's law of universal gravitation to these particles? We propose the idea that these particles may attract each other regardless of distance, resulting in a force that behaves exactly the same way as the force derived from presumed dark matter. Traces of such a force seem to be present in galaxies due to gamma ray bursts (GRBs) that produce entangled particles which hit various objects. We can observe that in barred spiral galaxies the arms always pass through the nucleus of the galaxy so we believe that the very first GRB happened at the central supermassive black hole (SMBH) and the arms are the traces of this ancient GRB. If we see an unbarred spiral galaxy, we can be certain that the arms do not pass through the core and we think the very first GRB happened close to the core. Ring galaxies may also be considered as a type of spiral galaxies, since there is a section where the ring is broken, i.e. where the arms do not meet. So the very first GRB happened far from the core. Elliptical galaxies may have resulted from an ancient GRB which hit from outside. The arms rotating in opposite directions of the NGC4622 galaxy support our hypothesis. Finally in the silk threads of the spider web of the universe, the traces of GRBs can be seen

Logisztikai manipulátor szerkezetének vizsgálata vezérlésének megtervezése

Logisztikai manipulátor szerkezetének vizsgálata vezérlésének megtervezéseBscMérnök Informatiku

Vanadium(III) binding strengths of small biomolecules

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Új, funkcionalizált peptidszármazékok előállítása és oldategyensúlyi vizsgálata = Synthesis and solution equilibrium studies of new, functionalised derivatives of peptides

A pályázat keretében 15 új peptidhidroxámsavat állítottunk elő és szisztematikusan megvizsgáltuk azt, hogy a ligandumok építőelemeinek (terminális aminocsoport jelenléte, a hidroxámsavcsoport nitrogénjének szubsztituense, a peptidlánc hossza, az oldalláncban jelenlevő erősen koordinálódni képes donorcsoport jelenléte) megváltoztatása hogyan befolyásolja fémionmegkötő képességüket. A ligandumok esszenciális (Fe3+, Cu2+, Ni2+, Zn2+, Mo(VI)) és toxikus (Al3+) fémionokkal való kölcsönhatásának tanulmányozására pH-potenciometriát, ESI-MS-t és spektrális módszereket (UV-VIS, NMR, CD, ESR) alkalmaztunk, meghatározva az oldatbeli részecskék összetételét, stabilitási szorzat értékeit és legvalószínűbb oldatszerkezetét. | Fifteen new peptide hydroxamic acids have been synthesized, characterized and a systematic study has been carried out to explore the effect of the change of the building blocks (presence of the terminal amino group, substituent at the nitrogen of the hydroxamic moiety, length of the peptide chain, presence of strongly coordinating donor in the side chain) of the ligands on their metal binding capability. The interaction of the peptide hydroxamic acids with essencial (Fe3+, Cu2+, Ni2+, Zn2+, Mo(VI)) and toxic (Al3+) metal ions has been studied using pH-potentiometry, ESI-MS and different spectroscopic (UV-VIS, NMR, CD, ESR) techniques

Interaction of iron(III) with taste enhancers:Potential of Fe(III) salts with inosine monophosphate or guanosine monophosphate for food fortification

Iron interactions in iron-fortified savory concentrates lead to undesirable discoloration, even when poorly-water soluble iron salts such as ferric pyrophosphate (Fe4PP3) are used. This is the first study to comprehensively investigate the interaction of Fe(III) with three common taste enhancers: glutamate (Glu), inosine monophosphate (IMP), and guanosine monophosphate (GMP). The stability of the complexes of Fe(III) with IMP or GMP is higher compared to that with Glu. Neutrality of IMP or GMP species with Fe(III) at pH 3–8 resulted in precipitation. This property was exploited to synthesize Fe(III) salts of IMP or GMP (i.e. Fe2IMP3 and Fe2GMP3) by aqueous chemical precipitation. Iron dissolution from Fe2IMP3 and Fe2GMP3 was up to twenty-fold higher at gastric pH (1–3), indicative of better bio-accessibility, and up to fifteen-fold lower at food pH (3–7), indicative of decreased reactivity in food, compared to Fe4PP3. Consequently, Fe2IMP3 and Fe2GMP3, compared to Fe4PP3, led to less discoloration in combination with the poorly soluble phenolics that are commonly present in savory concentrates. We conclude that Fe(III) salts of IMP or GMP can potentially serve as iron fortificants due to their increased solubility at gastric pH (1–3), decreased iron dissolution at food pH (3–7), and decreased reactivity at food pH.</p

Synthesis, characterization and albumin binding capabilities of quinizarin containing ternary cobalt(III) complexes

Four Co(III) ternary complexes with the composition of [(Co(4 N))2(quin)](ClO4)4 or [(Co(4 N))2(quinS)](ClO4)3, where 4 N = tris(2-aminoethyl)amine (tren) or tris(2-pyridylmethyl)amine (tpa), quinH2 = quinizarin (1,4-dihydroxy-9,10-anthraquinone), quinSH3 = quinizarin-2-sulfonic acid (1,4-dihydroxy-9,10-anthraquinone-2-sulfonic acid), were synthesized, characterized and their human serum albumin (HSA) binding capabilities were also tested. The complexes can be considered as likely chaperons of quinizarins which are structural models for anthracycline-based anticancer drugs like doxorubicin. All the Co(III) complexes are dinuclear and were isolated as mixture of isomers. Comparison of the cyclic voltammograms of the free ligands and the appropriate Co(III) complexes revealed that the new signals belonging to reversible processes in the range −400–0 mV (vs. Ag/AgCl) for the complexes can be attributed to the reversible reduction of the Co(III) centre. These potentials are in the range of typical (O,O) chelated Co(III) ternary complexes bearing 4 N donor ligands and follow the order being more positive for the tpa containing complexes. Presence of the sulfonate group in the quinizarin results in slightly more negative reduction potential of the Co(III) complexes. HSA binding capabilities of the quinH2 and quinSH3 ligands as well as the appropriate complexes showed that quinSH3 has higher affinity to the protein than quinH2 while none of the complexes seem to bind to HSA