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On the other hand, it’s only in the last few decades that we’ve come to realise that! Hypnosis itself hasn’t changed for millennia, but our understanding of it and our ability to control it has changed quite profoundly. The history of hypnosis, then, is really the history of this change in perception. In the 2. 1st century, there are still those who see hypnosis as some form of occult power. Those who believe that hypnosis can be used to perform miracles or control minds are, of course, simply sharing the consensus view that prevailed for centuries. Recorded history is full of tantalising glimpses of rituals and practices that look very much like hypnosis from a modern perspective, from the “healing passes” of the Hindu Vedas to magical texts from ancient Egypt. These practices tend to be for magical or religious purposes, such as divination or communicating with gods and spirits. It’s important to remember, however, that what we see as occultism was the scientific establishment of its day, with exactly the same purpose as modern science – curing human ills and increasing knowledge. From a Western point of view, the decisive moment in the history of hypnosis occurred in the 1. Century (coinciding with the Enlightenment and the Age of Reason). The work of Franz Mesmer, amongst others, can be seen as both the last flourish of “occult” hypnosis and the first flourish of the “scientific” viewpoint. Mesmer was the first to propose a rational basis for the effects of hypnosis. Although we now know that his notion of “animal magnetism”, transferred from healer to patient through a mysterious etheric fluid, is hopelessly wrong, it was firmly based on scientific ideas current at the time, in particular Isaac Newton’s theories of gravitation. Mesmer was also the first to develop a consistent method for hypnosis, which was passed on to and developed by his followers. It was still a very ritualistic practice. Mesmer himself, for instance, liked to perform mass inductions by having his patients linked together by a rope, along which his “animal magnetism” could pass. He was also fond of dressing up in a cloak and playing ethereal music on the glass harmonica whilst this was happening. The popular image of the hypnotist as a charismatic and mystical figure can be firmly dated to this time. Inevitably, these magical trappings led to Mesmer’s downfall, and for a long time, hypnotism was a dangerous interest to have for anybody looking for a mainstream career. Nevertheless, the stubborn fact remained that hypnosis worked, and the 1. Century is characterised by individuals seeking to understand and apply its effects. Surgeons and physicians like John Elliotson and James Esdaille pioneered its use in the medical field, risking their reputation to do so, whilst researchers like James Braid began to peel away the obscuring layers of mesmerism, revealing the physical and biological truths at the heart of the phenomenon. Thanks to their persistence and efforts, by the end of the century hypnosis was accepted as a valid clinical technique, studied and applied in the great universities and hospitals of the day. This trend continued into the 2. Century, although in some ways, hypnosis became imprisoned by its own respectability, as it became mired in endless academic debate about “state” or “non- state”. This conundrum – does hypnosis have a real, physical basis, or not? Important shifts were happening elsewhere, however. First of all, the centre of hypnotic gravity moved from Europe to America, where all the most significant breakthroughs of the 2. Secondly, hypnosis became a popular phenomenon, something that was increasingly available to the layman, outside of the laboratory or clinic. At the same time, the style of hypnosis changed, from a direct instruction issued by an authoritarian figure (a legacy of the charismatic mesmerist) to a more indirect and permissive style of trance induction, based on subtly persuasive language patterns. This was largely due to the work of therapists such as Milton H. Erickson. More importantly, perhaps, hypnosis became increasingly practical, and regarded as a useful tool for easing psychological distress and bringing about profound change in a variety of situations. This theme has continued up to the present day. Advances in neurological science and brain imaging, together with the work of British psychologists Joe Griffin and Ivan Tyrrell who linked hypnosis to the Rapid Eye Movement (REM), have also helped to resolve the “state/non- state” debate, bringing hypnosis and hypnotic trance firmly into the realm of everyday experience. At the same time, the nature of “ordinary” consciousness is better understood as a series of trance states that we go into and out of all the time. The history of hypnosis, then, is like the search for something that was in plain view all along, and we can now see it for what it is – a universal phenomenon that’s an inextricable part of being human. The future of hypnosis will be to fully realise the incredible potential of our natural hypnotic abilities. Langt de fleste enzymer kan klassifiseres kjemisk som enkle eller sammensatte proteiner. Et viktig eksempel finnes i ribosomene. Ofte har disse en lavmolekyl. Berzelius ordet katalysator om et stoff som f. Han beskrev hvordan en katalysator . Berzelius forsto ikke hvordan en katalysator virker. Kjemikere p. Kjemikerne trodde lenge at enzymene m. Buchner at en ekstrakt av knuste gj. Disse molekylene kaller vi kofaktorer. De fleste B- vitaminene fungerer som koenzymer. Den prostetiske gruppen kan ogs. For eksempel er jern- og kobberioner fast bundet i mange enzymer. Mangan- og sinkioner er andre, vanlige, prostetiske grupper av enzymer. Et enzym senker aktiveringsenergien mer effektivt enn en uorganisk katalysator. Dette kan illustreres med et naturlig eksempel. I kroppen blir det kontinuerlig dannet hydrogenperoksid (H2. O2) som et biprodukt i stoffskiftet. Men hydrogenperoksid er en gift for cellene og m. Det spaltes til vann og oksygengass. Reaksjonen har en aktiveringsenergi p. Med jernioner som uorganisk katalysator senkes aktiveringsenergien bare til 5. J/mol, men med enzymet katalase senkes aktiveringsenergien til 5. Det stoffet et enzym omdanner, blir kalt substrat. Substratet reagerer med enzymet og danner et mellomprodukt. Dette enzym- substrat- komplekset, ES, spaltes s. Deres aktivitet bestemmes af den tredimensionelle strukturen. Det er her ES- komplekset blir dannet. For at det aktive setet skal fungere trengs oftest et koenzym eller en prostetisk gruppe som bindeledd mellom substratet og proteindelen av enzymmolekylet. Det aktive setet utgj. Men denne modellen er for statisk til . For eksempel vil reaksjonen som katalyseres af enzymet orotidin 5'- fosfatdecarboxylase forbruke halvparten av en viss substratmengde p. I forbrenningen i cellene blir sluttproduktet CO2 dannet. Ved hjelp av karboanhydrase omdannes CO2- gassen til vannl. Uten enzymet blir bare ett molekyl CO2 omdannet i samme tidsrom. Aktiviteten til enzymer kan studeres p. Det er flere faktorer som p. De viktigste er: temperaturp. Hsubstratkonsentrasjonenzymhemmer (inhibitor)Ved lav temperatur g. Dette fordi molekylene som deltar i reaksjoen har st. Den temperaturen som reaksjonen g. Et enzym virker optimalt ved en bestemt temperatur. De fleste enzymene i menneskekroppen, har naturlig nok, en optimumstemperatur rundt 3. Enzymer i vaskemidler virker best ved 3. Ved temperatur over 6. Den optimale p. H- verdien er oftest rundt 7 for de reaksjonene som skjer i kroppen til et menneske. Enzymet pepsin i magesekken virker likevel best ved lav p. H, og den optimale p. H- verdien er 1,7. Ved store p. H- endringer skjer det en denaturering av de fleste enzymer. Pepsin bli denaturert ved p. H > 5. De fleste enzymer har optimum p. H mellom 4 og 1. 0. Konsentrasjonen av substratet har ogs. Dette skyldes at det blir lettere for enzym- og substratmolekylene . Fortsatt tilsetning av substrat etter at maksimumet er n. Dagens modeller for enzymkinetikk bygger p. Noen enzymer kan brukes p. Diagrammet viser relasjonen mellom substratkonsentrasjonen (S) og reaksjonshastigheten (v). For denne reaksjonen kunne de bekrefte hans formel, som han ikke selv fikk til . Denne formelen som gir sammenhengen mellom reaksjonshastigheten v og substratkonsentrasjonen . Molekylene som bindes kalles ligander. Hvor sterkt liganden binder uttrykkes som ligandens affinitet. Regulering av slik binding gj. Binding av ligand til ett sete kan ogs. Konsentrasjon av proteinet er en viktig type regulering. Det finnes ogs. Man kan for eksempel begrense tilgangen p. Denatureringen er i de fleste tilfeller irreversibel og enzymet er . Dette kalles reversibel hemning. Det er to former for reversibel hemning: . Hvis det er mye inhibitor til stede, vinner den i konkurransen, og enzymet blokkeres midlertidig. En . I stedet fester inhibitoren seg da til et annet sted p. En slik inhibitor kalles en enzymgift. Enzymgiften binder seg fast til enzymet og blokkerer det aktive setet. En annen beryktet enzymgift er cyanid (CN- ), som binder seg til det enzymet som katalyserer siste trinn i forbrenningen av glukose. Over 3 0. 00 forskjellige enzymer er blitt p. Etter hvert ble det vanlig . Lipase og laktase er ford. Andre enzymer katalyserer en gruppe substrater. Enzymene deles derfor inn i flere hovedgrupper. De to hovedgruppene er oksido- reduktaser (overf. Det er flere undergrupper, men oksidaser og dehydrogenaser er blant de viktigste. Oksidaser oksiderer en forbindelse (A- 2. H) ved at to H- atomer i forbindelsen blir overf. Dehydrogenaser oksiderer en forbindelse ved . Blant dehydrogenasene finnes alkoholdehydrogenase, som fjerner to H- atomer fra etanol. Isomeraser katalyserer isomeriseringen av et molekyl, for eksempel omdanningen av fruktose til glukose - begge med strukturformelen C6. H1. 2O6. De fleste enzymene er spesifikke med henzyn til den romlige strukturen av et substrat, slik at speilbildeisomeren av substratet ikke kan omdannes. Man har ogs. Disse spalter ulike molekyler under medvirkning av henholdsvis vann og fosforsyre. I dag har hvert enzym et systematisk navn og et nummer etter hvilken reaksjonstype og hvilket substrat det katalyserer. Navnsettingen reguleres ved anbefalinger fra International Union of Biochemistry and Molecular Biology. Det er utviklet et nummersystem, de s. Curr Opin Struct Biol, 1. The ribosome is a ribozyme. Science, 2. 89 (5. The importance of being selective. Nature, 3. 89 (6. Quoted in Manchester K. Trends Biotechnol, 1. Concepts in Biochemistry (2nd ed. New York, Chichester, Weinheim, Brisbane, Singapore, Toronto.: John Wiley & Sons, Inc. English translation Accessed 6 April 2. Download Audio Driver For Windows 7 Ultimate No Sound 3. Bits. Product was successfully added to your shopping cart. ASUS P6. T WS Professional Sound. MAX Audio Driver Download. Sound Cards; Modems.. 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Trying to ident and date a Contax IIa or IIIa. Discussion in 'Collector's Corner' started by Gizdan, Sep 6, 2009. Carlos Alberte, there are many lists of Zeiss serial numbers with dates of manufacture. What is your lens' serial number? As of 2016, the Leica pages get 3X more traffic and the Contax page traffic has plummeted. The Zeiss ZE and ZF lenses have effectively killed Contax interest. Serial Numbers; British Patents. This is a late example of the Contax I. Serial Number: Y96909 (c. The Contax was Zeiss-Ikon's first 35 mm. Anyone know of a web site which lists Contax/Zeiss lenses with their serial# range by focal length and date of manufacture? I can't seem to find this information and. Published in Autumn 2008 Zeiss Historica Journal. Author: Simon Worsley. Contax IIIa with gold serial number Contax No1. The last model Contax cameras had gold serial numbers on the flash shoe. The Zeiss Ikon Logo Contax No 13. Copyright. Zeiss Sample Case. In the mid- 1. 95. Zeiss Ikon Stuttgart began offering dealers 'display sample cases'. Contax IIa IIIa serial numbers :: Film :: Home :: Film Rangefinder / Viewfinder Cameras.Some people wrongly call these salesman's sample cases. Zeiss started promoting the full range of Contax items using these cases around April 1. Cases were also offered for Contina III, Contaflex, and probably other Zeiss systems. The interiors were attractively lined in velvet. The inside top fabric was embossed with the Zeiss Ikon logo. Cases came with a full range of Contax interchangeable lenses, filters, viewfinders, and cameras (probably one camera came with the case). Zeiss offered the case to dealers free of charge with a 5 percent discount on all accessories. Discounts were also offered to the dealer on the cameras if they were ordered to fill out the set. Zeiss suggested dealers use these cases as an appealing way to promote Contax sales. Obviously this did not work well enough as camera production ceased in 1. Zeiss is still in business and makes optics. Contax Cameras and Accessories. Before WWII plants in Dresden, Jena, and Stuttgart had several thousand workers. Once the war ended the remains of the plants under Russian control were reassembled. A new Zeiss Ikon factory was set up in Stuttgart. Introduced around March 1. Contax IIa and IIIa were beautifully made machines. The post- war cameras were more refined, better machined, and smaller than the pre- war Contax cameras. There were two versions of the IIa and IIIa Contax cameras. The black dial camera (the speed dial is all lettered in black) needed a special sync cord for the flash (1. The red dial camera (the later camera) had a modern day PC fitting for electronic flash. Zeiss Biogon lens. Contax No. 3A sharp ultra- wide lens. It had a 9. 0 degree angle of view, 8 elements, and focused to 3 feet. These levels were beautifully turned on a lathe and heavily metal plated. It had hanging frame lines for each of the lenses. If you bumped your camera too hard then the meter could be knocked off the pivots which was expensive to fix. Don't attempt to take one of these apart ever! Contax IIa circa 1. Contax No 1. 0This is a IIa red dial camera. The Zeiss turret finder is pictured on top of the camera. Attempt at airplane picture. Contax No 1. 1Zeiss Ikon Dealer Sign. Contax No. 12. This is a rare sign that you will seldom see. The Zeiss Ikon Logo. Contax No 1. 3The Factory as it looked in early 1. Contax No 1. 4Optics marked . Contax II and III copies marked Kiev were made in central Russia with an entire factory rail shipped from Jena. These optics are normally the ones that collectors desire. Contax Zeiss Serial#/YR of Manufacture. I believe the definitive reference is sold by camerabooks. Fabrikationsbuch Photooptik III. Carl Zeiss Oberkochen 1. Edition by Hartmut Thiele. It'll cost you $5. German. The synopsis reads as follows: The production started in Oberkochen in the year of 1. 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Copy and paste or type in manually whatever text you want reversed or flipped or one click tweet to all of your followers. PRIVACY NOTICE: All data is converted on client- side browsers and no data entered is saved by this site. Tweet. Backwards - Spell. Backwards#Thank. Me. Spell or Tweet Backwards with this quick generator tool. Copy and paste or type in manually whatever text you want reversed or flipped. Later: @Rey. Haynes. Crystal structure of a Kir. Kir channel chimera - Nishida - 2. The EMBO Journal. Introduction. Inward rectifier K+ channels (Kir channels) comprise one family of K+ selective ion channels. Kir. 1 channels are important for electrolyte flow across kidney epithelial cells (Hebert et al, 2. Kir. 2 channels control the resting membrane potential in many different cells and are important for electrical activity in muscle and neurons (Stanfield et al, 2. In cardiac atrial cells, Kir. What is the difference between prokaryotic and eukaryotic. 209-3 Use a light microscope or micro-viewer correctly to produce. Plant and Animal Cell Worksheets. Plant cell walls are designed for the process of photosynthesis. Plant cells chloroplasts, a large vacuole. GIRK channels, are responsible for slowing the heart rate when the vagus nerve is stimulated and for membrane potential maintenance in certain neurons (Stanfield et al, 2. Kir. 6 channels, which exist as a complex with a second membrane protein called the sulfonylurea receptor, are regulated by the intracellular concentration of ATP (Aguilar- Bryan et al, 1. In pancreatic beta cells, this form of regulation allows Kir. Ashcroft, 2. 00. 6). These cellular functions underscore the medical importance of Kir channels. Familial diseases characterized by abnormal electrolyte processing by the kidney, epilepsy, cardiac arrhythmia and diabetes mellitus have their basis in abnormal function of Kir channels (Simon et al, 1. Plaster et al, 2. Hattersley and Ashcroft, 2. Thus, Kir channels are potentially important targets for pharmaceutical agents. The name . This is because Mg. K+ (Matsuda et al, 1. Vandenberg, 1. 98. Lopatin et al, 1. Consequently Kir channels operate near the resting membrane potential and tend to be silenced when voltage- dependent Na+ or Ca. Kir channels, like other K+ channels, are tetramers of identical or similar subunits that surround a central ion conduction pathway. Each subunit contains two transmembrane . The N- and C- termini, which are located on the intracellular side of the membrane, form a large . Electrophysiological studies show that the cytoplasmic pore is important for at least two purposes. First, it extends the effective length of the pore. The extra long pore contains some of the acidic residues essential for blockage of the channel by Mg. Question: Write down the difference between Prokaryotic Cell and Eukaryotic Cell? Mitosis & Meiosis > Replication/Transcription/Translation. Replication is the process in which a cell makes an exact copy of its own DNA. They also parasitize the cell for basic. While the double-stranded DNA is responsible for this in prokaryotic and eukaryotic. By producing a chimera between prokaryotic and eukaryotic. Unit cell: 45.27 47.64. Of further structural differences between eukaryotic and. A prominent difference between the RbcL binding sites of AtRbcX1 and. Taglialatela et al, 1. Yang et al, 1. 99. Guo and Lu, 2. 00. Second, the cytoplasmic pore is the structural component through which gating of Kir channels can be modulated by regulatory proteins, ATP, Na+ ions or p. H (Stanfield et al, 2. Hebert et al, 2. 00. Ashcroft, 2. 00. 6). Opening of Kir. 3 channels, for example, is stimulated by beta–gamma G- protein subunits (Logothetis et al, 1. Reuveny et al, 1. Wickman et al, 1. Another prominent feature of Kir channels is their regulation by the signaling lipid phosphotidylinositol 4,5- bisphosphate (PIP2) (Hilgemann and Ball, 1. Baukrowitz et al, 1. Huang et al, 1. 99. Shyng and Nichols, 1. Liou et al, 1. 99. Zhang et al, 1. 99. Lopes et al, 2. 00. Pegan et al, 2. 00. In Kir. 3 channels, there is a complex interplay between the effects on gating of beta–gamma G- protein subunits and PIP2: both appear to be important for channel opening through direct interactions with the ion channel (Huang et al, 1. Recently, three crystallographic studies have provided information on Kir structures. The cytoplasmic pores of Kir. Kir. 2. 1 have been described at 1. The cytoplasmic pore structures correspond to the eukaryotic channels that have been studied extensively for many years using electrophysiological methods, but they are detached from the transmembrane pore. The prokaryotic channel structure, although complete, is only 1. Kir. 3. 1. In combination, these structures have provided templates for homology models for interpreting functional data on eukaryotic Kir channels (Antcliff et al, 2. In this study, we have determined two structures at high resolution (2. The eukaryotic component encompasses the regulatory surfaces through which Kir. G- protein subunits and signaling lipids. Many disease- causing mutations map to these surfaces. Results and discussion. Structure of the chimeric channel. Figure 1. A shows an amino- acid sequence alignment that includes four eukaryotic channels representing different subclasses of eukaryotic Kir channels, Kir. Bac. 1. 3 and a prokaryotic K+ channel from Streptomyces lividans (Kcs. A). We produced a chimeric channel by splicing Kir. Kir. Bac. 1. 3 at the indicated junctions (Figure 1. A and B). The N- terminus of Kir. Bac. 1. 3 was retained in order to achieve correct processing and membrane insertion using the Escherichia coli expression system. This N- terminus was then removed by thrombin cleavage before crystallization, whereas the N- terminal region of Kir. K4. 1 in the Kir. The transmembrane helix junction points were constructed sufficiently deep within the membrane to ensure that all of the cytoplasmic and membrane- surface exposed regions of the channel are of eukaryotic origin. In particular, the interfacial helix (lying parallel to the membrane plane, termed the slide helix in Kuo et al, 2. Kir. 3. 1. Numerous electrophysiological studies have shown that the eukaryotic components, colored blue in Figure 1. B, are important for gating and regulation of Kir channels (Stanfield et al, 2. Hebert et al, 2. 00. Ashcroft, 2. 00. 6).(A) Sequence alignment of the chimera and K+ ion channels from mammals and prokaryotes. Abbreviations are as follows: Kir. Kir. 3. 1, Kir. 1. Kir. 1. 1, Kir. 2. Kir. 2. 1, Kir. 6. Kir. 6. 2. Notation for secondary structures and numbering for the chimera above the sequences are from the published structure of the Kir. Nishida and Mac. Kinnon, 2. The regions from Kir. Kir. Bac. 1. 3 in the chimeric channel are colored blue and red, respectively. Highly conserved residues are colored cyan. Signature sequence residues (1. G- loop residues (3. Only two subunits are shown for clarity. The linker region between the N- terminus and the interfacial helix (dotted line) is disordered and not resolved. Boundaries of the lipid bilayer are drawn as yellow bars. The chimera (red) and Kcs. A (black) are superposed. The interfacial helix of the chimera is omitted. Construction of the chimeric channel that expressed as a stable membrane protein was not straightforward and required many attempts (Supplementary Figure S1). This fact suggests that there are strict structural requirements, such as achieving the proper phase of the helix attachments. Moreover, we were unable to construct a similar chimera using the pore of the Kcs. A K+ channel, which is not a member of the Kir family. The strict constraints on establishing a . Crystallization at p. H 6. 2 in 1. 20 m. M KCl, 2. 00 m. M potassium phosphate and polyethylene glycol 4. X- rays to 2. 2 . The tetragonal crystal contained two unique subunits per asymmetric unit, allowing the structure determination of two unique four- fold symmetric chimeric channels, each revealing a different conformation of the cytoplasmic pore. The transmembrane pores are essentially identical to each other. One of these transmembrane pores is compared in Figure 1. C with the corresponding region of Kcs. A. Table 1. Data and refinement statistics. Data statistics Space group. P4 Lattice constants (. A crystal soaked in Rb. Cl was used to identify permeant ions in the conduction pathway (see Materials and methods). Four ion positions are observed in the selectivity filter, a fifth in the central cavity, and a sixth and seventh in between the transmembrane and cytoplasmic pores. Ion positions labeled 1 through 5 in Figure 2. A correspond to ions observed in Kcs. A (Zhou et al, 2. Ion positions labeled 6 and 7 are unique.(A) Conduction pore of the chimeric channel in the dilated conformation. A crystal was soaked in a Rb. Cl- containing solution before data collection. The structure refinement and subsequent map calculation were carried out at 2. Seven Rb+ ions (green spheres) were located on the Fo–Fc omit map contoured at 3. Two constriction sites along the pore (F1. C. Two subunits have been removed from the tetramer for clarity. The electrostatic potential of the surface was calculated using the program GRASP. The range of surface potentials is from . Electropositive and electronegative surfaces are colored blue and red, respectively. Part of the channel has been removed to expose the cytoplasmic pore's inner surface to the viewer. The channel contains two relatively constricted regions along its length (Figure 2. A, red). One of these constrictions corresponds to the inner helix bundle . Phenylalanine side chains completely occlude the pore at this point, suggesting that the inner helix bundle gate is closed. The closed gate is similar to that observed in Kir. Bac. 1. 1 (Kuo et al, 2. The second constriction occurs at the apex of the cytoplasmic pore. The cytoplasmic pore is electronegative inside, and therefore it should be attractive to cations such as K+, Mg. The abundant positively charged arginine and lysine amino acids on these surfaces are well positioned to interact with the negatively charged phospholipid head groups of the cell membrane's inner leaflet. Structural conservation in the K+ selectivity filter. Among the several K+ channel structures determined, Kcs. A has yielded the most detailed description at a resolution better than 2. The chimeric channel presented in this study at 2. Given that Kir channels and Kcs. A are far removed from each other on the K+ channel family tree, it is interesting to ask how highly conserved is the three- dimensional structure of the selectivity filter. The signature sequence amino acids, which form the first layer of atoms surrounding the K+ ions in the selectivity filter, are highly conserved in all K+ channels (Figure 1. A). But there is significant variation in nearby amino acids, particularly those forming the intricate protein core surrounding the selectivity filter (sequence labeled . K+ ions (green) and waters (red) are shown as spheres. Residues 1. 43–1. K+ ions and water molecules were omitted during simulated- annealing refinement against the native data set and subsequent map calculation at 2. The map is contoured at 1. Only two subunits are shown for clarity. |
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