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The mysterious advances in biochemical engineering biotechnology volume biomethanation ii in Europe paused upon them Still, but the free scales.
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The idea proposed in a could be directly tested with this setup these is hydrophobic as proposed by Walker and colleagues [12]. So the idea is that the inside of the sleeve without electrostatic interaction is very slippery. As a result, internal friction between the shaft and cylinder may be minimized with this kind of architecture.

Advances in Biochemical Engineering & Biotechnology, Volume 082, Biomethanation II

With this concept, what is the molecular mechanism of rotation in F1-ATPase? One may think that the shaft is closely packed within the cylinder in an asymmetric manner, and some push and pull motions of three catalytic cores cf. If this is the case, these conformational changes could be detected as an angular change of these domains. Tomoko Masaike in our group carefully chose the helix in the C-terminal domain of the catalytic subunit, which was assumed to be very mobile in line with the chemical state in the g-subunit, and labeled the specific region with a single fluorophore red in Fig. Note that we used a fluorescent probe that has two functional groups.

By reacting these two functional groups with two cysteines in the helix, the absorption transition moment of the fluorophore is perfectly aligned to the orientation of the single helix. The polarization of the evanescent field is modulated with time only in the xy-plane. Quarter-wave plate QWP rotates with the prism in sync by using a hollow motor To determine the orientation of the single fluorophore directly, we exploited an advanced type of TIRFlM, in which the polarization of evanescent fields is modulated with time Fig.

Suppose the single fluorophore is fixed in one orientation; its intensity is expected to show maximal and minimal when the excitation polarization becomes parallel and orthogonal, respectively, to absorption transition moment of the fluorophore. Therefore the intensity should oscillate as a sinusoidal wave. In the case that the angle of the fluorophore is changed, the phase of the signal should also be changed, indicating the fluorophore orientation. From this phase shifting, the angular change of the specific helix in the single protein molecule could be determined directly [5].

The rotation of the g-shaft was also observed simultaneously, with the different wavelength of the light to illuminate the beads as the light source of a dark-field microscope Fig.

Original Research ARTICLE

We used the hybrid F1-ATPase, in which only one b-subunit is mutant and has an extremely slow rate for hydrolysis [13]. The implication is that large domain motion occurs only when chemical reactions biding of ATP, cleavage of ATP, and release of ADP proceed in the fluorophore-labeled b-subunit.

Therefore, it is concluded that a b-subunit in F1-ATPase undergoes a three-step large motion of the C-terminal domain in relation to the N-terminal domain over 14 T. Substeps have been proposed in various mutants and now established as the common mechanism for rotation [5, 13, 14] one revolution of g-shaft.

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This is the first report to show the correlation between the chemical state and structural change of a protein, revealed directly at the single molecular level. Please note that what we are observing is the structure of only one fluorophorelabeled b-subunit. With these motions, the g-shaft rotates by one third. Note that during this unitary step, all three b-subunits are correlated with rotational motion of the g-shaft.

References 1. By the late s it had been shown that specific filterable viruses were the causative agents of some diseases in plants, some cancerous growth in animals, and of the lysis of some bacterial species. One of these viruses, causing the tobacco plant mosaic TMV disease, had been isolated in crystalline form by W. Stanley in [1]. All cells contain double-stranded DNA as their genetic material. This makes for interesting schemes of replication and gene expression. Many viruses are known that infect Bacteria and increasing numbers are known that infect Archaea.

I want to focus on three bacteriophages — T4 phage virulent virus , lambda phage template virus and filamentous phage not harmful to host. The study of genetic materials of virus has led to tremendous progress so that we can transfer the foreign genetic information to the cells that we want to manipulate and open the field of genetic engineering for the results to be used in bioindustry. Therefore I will not talk about the genome of bacteriophages but rather discuss the structural features of these bacteriophages in this article.

Hershey in the late s. Their meeting in marked the origin of the Phage Group. To see the structure of virus particles, we need an electron microscope. From the beginning, Thomas F. Anderson, one of the first American electron microscopists, was a member of this group. Therefore the structure of the bacteriophage was explored extensively [4]. Delbruck finally agreed that the phages are adsorbed by the tips of their tails and that none of the particles seem to enter the bacteria or their ghosts Other critical evidence was shown by the so-called Hershey, Chase experiment [5].

He described the experiment as follows.

Anderson had found that stirring the cell suspension in a blender prevented attachment of phage particles to bacteria, and perhaps Case and I Hershey should Molecular Biology and Biotechnology of Bacteriophage 19 have thought of using that machine first. Instead, we tried various grinding arrangements, with results that were not very encouraging.

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But when Margaret McDonald loaned us her blender, the experiments quickly succeeded. A chilled suspension of bacterial cells recently infected with phage T2 is spun for a few minutes in a blender and afterwards centrifuged briefly at a speed sufficient to throw the bacterial cells to the bottom of the tube. One thus obtains two fractions: a pellet containing the infected bacteria and a supernatant fluid containing any particles smaller than bacteria. Each of these fractions is analyzed for the radiophosphorus in DNA or radiosulfur in protein with which the original phage particles have been labeled.

The results are: 1. Most of the phage DNA remains with the bacterial cells 2. Most of the phage protein is found in the supernatant fluid 3.


Most of the initially infected bacteria remain competent to produce phage 4. If the mechanical stirring is omitted, both protein and DNA a sediment with the bacteria 5. The phage protein removed from the cells by stirring consists of more-or-less intact, empty phage coats, which may therefore be thought of as passive vehicles for the transport of DNA from cell to cell which, having performed that task, play no further role in phage growth At present it is fair to say that bacteriophage injected their DNA into the host cell and bacteria produced virus particles through the subtle interaction between bacteria and phage genome.

However, the mechanism of entry of animal virus into the host cell is quite different from that of bacteriophage. The entry of influenza virus is described as follows.

The influenza virus nucleocapsid is of helical symmetry, about 6—9 nm in diameter and about 60 nm long. This nucleocapsid is embedded in an envelope that has a number of virus-specific proteins as well as lipid derived from the host. Because of the way influenza virus buds as it leaves the cell, the virus has no defined shape and is said to be polymorphic. There are proteins on the outside of the envelope that interact with the host cell surface. One of these is called hemagglutinin, so named because it causes agglutination of red blood cells.

The red blood cell is not the type of host cell the virus normally infects, but contains on its surface the same type of membrane component, sialic acid, that the mucous membrane cells of the respiratory tract contain.


Thus, the red blood cell is merely a convenient cell type for assaying agglutination activity. An important feature of the influenza virus hemagglutinin is that antibodies directed against this hemagglutinin prevent the virus from infecting a cell. A second type of protein on the influenza virus surface is an enzyme called neuraminidase. This enzyme breaks down the sialic acid component of the cytoplasmic membrane, which is a derivative of neuraminic acid.

Neuraminidase appears to function primarily in the virus assembly process, destroying host membrane sialic acid that would otherwise block assembly or become incorporated into the mature virus particle. It is helpful to choose simple paradigms to represent more complex systems. Onodera The relative simplicity of the bacteriophage and of its bacterial host played an important role in the development of molecular biology. Therefore I want to choose three bacteriophages — T4 phage, lambda l phage and filamentous phage. I also want to discuss the molecular biology of these phages from the viewpoint of their structure and application of the results obtained from study of the structure to the biotechnology.

Chemical analyses of the total T-even phage protein did not bring to light any facts; its amino acid composition resembles more or less that of the total E. The phage protein is composed of at least five different types of polypeptides, of which the head protein makes up by far the major part.

Each of the tail components — sheath, tube, base plate, tail pins, and tail fibers — contains one or more specific polypeptides. Chemical analysis of the phage DNA did show the difference. Instead of cytosine, it contains the cytosine analog 5-hydroxymethylcytosine HMC. The one-step growth experiment demonstrated that the progeny of the infecting phage particle appear after a period of constant phage titer. The one-step growth experiment is a basic procedure for studying phage multiplication. A dense suspension of growing bacteria is infected with phages, incubated for a few minutes to allow most of the phage particles to attach themselves to the bacteria, and then diluted with nutrient medium to a concentration that may range from one ten-thousandth to one millionth that of the suspension.

The diluted culture is incubated further and samples plated on sensitive bacteria from time to time for plaque assay of the instantaneous number of infective units in the culture. The protocol and the results of a typical one-step growth experiment are shown in Fig. The number of plaque-forming units in the culture remains constant for the first 24 min after infection. This initial period is the latent period. After some 24 min have elapsed, the number of plaque-forming units in the culture Fig.