1.
Histology
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Histology is the study of the microscopic anatomy of cells and tissues of plants and animals. It is commonly performed by examining cells and tissues under a microscope or electron microscope, the specimen having been sectioned, stained. Histological studies may be conducted using tissue culture, where human or animal cells are isolated and maintained in an artificial environment for various research projects. The ability to visualize or differentially identify microscopic structures is frequently enhanced through the use of histological stains, histology is an essential tool of biology and medicine. Trained physicians, frequently licensed pathologists, are the personnel who perform histopathological examination and their field of study is called histotechnology. In the 17th century, Italian Marcello Malpighi invented one of the first microscopes for studying tiny biological entities, Malpighi analysed several parts of the organs of bats, frogs and other animals under the microscope. Malpighi, while studying the structure of the lung, noticed its membranous alveoli and his discovery established how the oxygen we breathe enters the blood stream and serves the body. In the 19th century, histology was a discipline in its own right. The French anatomist Bichat introduced the concept of tissue in anatomy in 1801, the 1906 Nobel Prize in Physiology or Medicine was awarded to histologists Camillo Golgi and Santiago Ramon y Cajal. They had dueling interpretations of the structure of the brain based in differing interpretations of the same images. Cajal won the prize for his theory and Golgi for the staining technique he invented to make it possible. There are four types of animal tissues, muscle tissue, nervous tissue, connective tissue. All tissue types are subtypes of these four basic tissue types and their structure is very different from animal tissues. The most common fixative for light microscopy is 10% neutral buffered formalin, for electron microscopy, the most commonly used fixative is glutaraldehyde, usually as a 2. 5% solution in phosphate buffered saline. These fixatives preserve tissues or cells mainly by irreversibly cross-linking proteins and this can be detrimental to certain histological techniques. Further fixatives are often used for electron microscopy such as osmium tetroxide or uranyl acetate Formalin fixation leads to degradation of mRNA, miRNA and DNA in tissues, however, extraction, amplification and analysis of these nucleic acids from formalin-fixed, paraffin-embedded tissues is possible using appropriate protocols. Frozen section procedure is a way to fix and mount histology sections using a refrigeration device called a cryostat. It is often used after surgical removal of tumors to allow determination of margin
2.
Epidermis
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The epidermis is the outer of the two layers that make up the skin, the inner layer being the dermis. It provides a barrier to infection from pathogens and regulates the amount of water released from the body into the atmosphere through transepidermal water loss. The outermost part of the epidermis is composed of stratified layers of flattened cells, the epidermis has no blood supply and is nourished almost exclusively by diffused oxygen from the surrounding air. It is 95% keratinocytes but also contains melanocytes, Langerhans cells, Merkel cells, rete ridges are epidermal thickenings that extend downward between dermal papillae. Blood capillaries are found beneath the epidermis, and are linked to an arteriole, the epidermis is composed of 4 or 5 layers depending on the region of skin being considered. Those layers in descending order are, cornified layer Composed of 10 to 30 layers of polyhedral, anucleated corneocytes, with the palms, most of the barrier functions of the epidermis localize to this layer. Clear/translucent layer The skin found in the palms and soles is known as thick skin because it has 5 epidermal layers instead of 4, granular layer Keratinocytes lose their nuclei and their cytoplasm appears granular. Lipids, contained into those keratinocytes within lamellar bodies, are released into the space through exocytosis to form a lipid barrier. Those polar lipids are then converted into non-polar lipids and arranged parallel to the cell surface, for example glycosphingolipids become ceramides and phospholipids become free fatty acids. Langerhans cells, immunologically active cells, are located in the middle of this layer, Composed mainly of proliferating and non-proliferating keratinocytes, attached to the basement membrane by hemidesmosomes. Melanocytes are present, connected to numerous keratinocytes in this and other strata through dendrites, Merkel cells are also found in the stratum basale with large numbers in touch-sensitive sites such as the fingertips and lips. They are closely associated with cutaneous nerves and seem to be involved in light touch sensation, the term Malpighian layer is usually defined as both the stratum basale and stratum spinosum. The epidermis is separated from the dermis, its underlying tissue, the stratified squamous epithelium is maintained by cell division within the stratum basale. Differentiated keratinocytes secrete keratin proteins which contribute to the formation of a matrix and is an integral part of the skin barrier function. The entire epidermis is replaced by new growth over a period of about 48 days. Calcium concentration in the stratum corneum is very low in part because those relatively dry cells are not able to dissolve the ions and this calcium gradient parallels keratinocyte differentiation and as such is considered a key regulator in the formation of the epidermal layers. Elevation of extracellular calcium concentrations induces an increase in intracellular free calcium concentrations, moreover, it has been suggested that an extracellular calcium-sensing receptor also contributes to the rise in intracellular calcium concentration. Epidermal organogenesis, the formation of the epidermis, begins in the covering the embryo after neurulation
3.
Optical microscope
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The optical microscope, often referred to as light microscope, is a type of microscope which uses visible light and a system of lenses to magnify images of small samples. Optical microscopes are the oldest design of microscope and were invented in their present compound form in the 17th century. Basic optical microscopes can be simple, although there are many complex designs which aim to improve resolution. The image from a microscope can be captured by normal light-sensitive cameras to generate a micrograph. Originally images were captured by photographic film but modern developments in CMOS, purely digital microscopes are now available which use a CCD camera to examine a sample, showing the resulting image directly on a computer screen without the need for eyepieces. Alternatives to optical microscopy which do not use visible light include scanning electron microscopy, there are two basic types of optical microscopes, simple microscopes and compound microscopes. A simple microscope is one which uses a lens for magnification. A compound microscope uses several lenses to enhance the magnification of an object, the vast majority of modern research microscopes are compound microscopes while some cheaper commercial digital microscopes are simple single lens microscopes. Compound microscopes can be divided into a variety of other types of microscopes which differ in their optical configurations, cost. A simple microscope uses a lens or set of lenses to enlarge an object through angular magnification alone, the use of a single convex lens or groups of lenses are still found in simple magnification devices such as the magnifying glass, loupes, and eyepieces for telescopes and microscopes. A compound microscope uses a close to the object being viewed to collect light which focuses a real image of the object inside the microscope. That image is magnified by a second lens or group of lenses that gives the viewer an enlarged inverted virtual image of the object. The use of a compound objective/eyepiece combination allows for higher magnification. Common compound microscopes often feature exchangeable objective lenses, allowing the user to quickly adjust the magnification, a compound microscope also enables more advanced illumination setups, such as phase contrast. There are many variants of the optical microscope design for specialized purposes. Comparison microscope, which has two light paths allowing direct comparison of two samples via one image in each eye. Inverted microscope, for studying samples from below, useful for cell cultures in liquid, student microscope, designed for low cost, durability, and ease of use. Polarizing microscope, similar to the petrographic microscope, phase contrast microscope, which applies the phase contrast illumination method
4.
Microscopy
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Microscopy is the technical field of using microscopes to view objects and areas of objects that cannot be seen with the naked eye. There are three branches of microscopy, optical, electron, and scanning probe microscopy. This process may be carried out by irradiation of the sample or by scanning of a fine beam over the sample. Scanning probe microscopy involves the interaction of a probe with the surface of the object of interest. The development of microscopy revolutionized biology, gave rise to the field of histology and so remains an essential technique in the life and physical sciences. Optical or light microscopy involves passing visible light transmitted through or reflected from the sample through a single or multiple lenses to allow a view of the sample. The resulting image can be detected directly by the eye, imaged on a plate or captured digitally. The single lens with its attachments, or the system of lenses and imaging equipment, along with the lighting equipment, sample stage and support. The most recent development is the microscope, which uses a CCD camera to focus on the exhibit of interest. The image is shown on a screen, so eye-pieces are unnecessary. Limitations of standard optical microscopy lie in three areas, This technique can only image dark or strongly refracting objects effectively, diffraction limits resolution to approximately 0.2 micrometres. This limits the practical limit to ~1500x. Out of focus light from points outside the focal plane reduces image clarity, live cells in particular generally lack sufficient contrast to be studied successfully, since the internal structures of the cell are colourless and transparent. The most common way to increase contrast is to stain the different structures with selective dyes, staining may also introduce artifacts, apparent structural details that are caused by the processing of the specimen and are thus not legitimate features of the specimen. In general, these make use of differences in the refractive index of cell structures. It is comparable to looking through a window, you dont see the glass. There is a difference, as glass is a material. The human eye is not sensitive to this difference in phase, in order to improve specimen contrast or highlight certain structures in a sample special techniques must be used
5.
Fluorescence microscope
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The specimen is illuminated with light of a specific wavelength which is absorbed by the fluorophores, causing them to emit light of longer wavelengths. The illumination light is separated from the much weaker emitted fluorescence through the use of an emission filter. Typical components of a microscope are a light source, the excitation filter, the dichroic mirror. The filters and the dichroic beamsplitter are chosen to match the spectral excitation and emission characteristics of the used to label the specimen. In this manner, the distribution of a fluorophore is imaged at a time. Multi-color images of types of fluorophores must be composed by combining several single-color images. Most fluorescence microscopes in use are epifluorescence microscopes, where excitation of the fluorophore and these microscopes are widely used in biology and are the basis for more advanced microscope designs, such as the confocal microscope and the total internal reflection fluorescence microscope. The majority of fluorescence microscopes, especially used in the life sciences, are of the epifluorescence design shown in the diagram. Light of the wavelength is focused on the specimen through the objective lens. Fluorescence microscopy requires intense, near-monochromatic, illumination which some widespread light sources, four main types of light source are used, including xenon arc lamps or mercury-vapor lamps with an excitation filter, lasers, supercontinuum sources, and high-power LEDs. In order for a sample to be suitable for fluorescence microscopy it must be fluorescent, there are several methods of creating a fluorescent sample, the main techniques are labelling with fluorescent stains or, in the case of biological samples, expression of a fluorescent protein. Alternatively the intrinsic fluorescence of a sample can be used, as a result, there is a diverse range of techniques for fluorescent staining of biological samples. Many fluorescent stains have been designed for a range of biological molecules, some of these are small molecules which are intrinsically fluorescent and bind a biological molecule of interest. Major examples of these are nucleic acid stains like DAPI and Hoechst and DRAQ5 and DRAQ7 which all bind the minor groove of DNA, others are drugs or toxins which bind specific cellular structures and have been derivatised with a fluorescent reporter. A major example of class of fluorescent stain is phalloidin which is used to stain actin fibres in mammalian cells. Immunofluorescence is a technique which uses the specific binding of an antibody to its antigen in order to label specific proteins or other molecules within the cell. A sample is treated with an antibody specific for the molecule of interest. A fluorophore can be conjugated to the primary antibody
6.
Fluorescence
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Fluorescence is the emission of light by a substance that has absorbed light or other electromagnetic radiation. It is a form of luminescence, in most cases, the emitted light has a longer wavelength, and therefore lower energy, than the absorbed radiation. Fluorescent materials cease to glow immediately when the radiation source stops, unlike phosphorescence, Fluorescence also occurs frequently in nature in some minerals and in various biological states in many branches of the animal kingdom. An early observation of fluorescence was described in 1560 by Bernardino de Sahagún and it was derived from the wood of two tree species, Pterocarpus indicus and Eysenhardtia polystachya. The chemical compound responsible for this fluorescence is matlaline, which is the product of one of the flavonoids found in this wood. The name was derived from the fluorite, some examples of which contain traces of divalent europium. In a key experiment he used a prism to isolate ultraviolet radiation from sunlight, the specific frequencies of exciting and emitted light are dependent on the particular system. S0 is called the state of the fluorophore, and S1 is its first excited singlet state. A molecule in S1 can relax by various competing pathways and it can undergo non-radiative relaxation in which the excitation energy is dissipated as heat to the solvent. Excited organic molecules can also relax via conversion to a triplet state, relaxation from S1 can also occur through interaction with a second molecule through fluorescence quenching. Molecular oxygen is an extremely efficient quencher of fluorescence just because of its unusual triplet ground state, in most cases, the emitted light has a longer wavelength, and therefore lower energy, than the absorbed radiation, this phenomenon is known as the Stokes shift. The emitted radiation may also be of the wavelength as the absorbed radiation. Molecules that are excited through light absorption or via a different process can transfer energy to a second sensitized molecule, the fluorescence quantum yield gives the efficiency of the fluorescence process. It is defined as the ratio of the number of photons emitted to the number of photons absorbed, Φ = Number of photons emitted Number of photons absorbed The maximum fluorescence quantum yield is 1.0, each photon absorbed results in a photon emitted. Compounds with quantum yields of 0.10 are still considered quite fluorescent, thus, if the rate of any pathway changes, both the excited state lifetime and the fluorescence quantum yield will be affected. Fluorescence quantum yields are measured by comparison to a standard, the quinine salt quinine sulfate in a sulfuric acid solution is a common fluorescence standard. The fluorescence lifetime refers to the time the molecule stays in its excited state before emitting a photon. This is an instance of exponential decay, various radiative and non-radiative processes can de-populate the excited state
7.
Dye
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A dye is a colored substance that has an affinity to the substrate to which it is being applied. The dye is applied in an aqueous solution, and may require a mordant to improve the fastness of the dye on the fiber. Both dyes and pigments are colored because they absorb some wavelengths of light more than others, in contrast to dyes, pigments are insoluble and have no affinity for the substrate. Some dyes can be precipitated with a salt to produce a lake pigment. The majority of natural dyes are from plant sources, roots, berries, bark, leaves, and wood, fungi, textile dyeing dates back to the Neolithic period. Throughout history, people have dyed their textiles using common, locally available materials, scarce dyestuffs that produced brilliant and permanent colors such as the natural invertebrate dyes Tyrian purple and crimson kermes were highly prized luxury items in the ancient and medieval world. Plant-based dyes such as woad, indigo, saffron, and madder were raised commercially and were important trade goods in the economies of Asia, across Asia and Africa, patterned fabrics were produced using resist dyeing techniques to control the absorption of color in piece-dyed cloth. Dyes from the New World such as cochineal and logwood were brought to Europe by the Spanish treasure fleets, dyed flax fibers have been found in the Republic of Georgia in a prehistoric cave dated to 36,000 BP. Archaeological evidence shows that, particularly in India and Phoenicia, dyeing has been carried out for over 5,000 years. The dyes were obtained from animal, vegetable or mineral origin, by far the greatest source of dyes has been from the plant kingdom, notably roots, berries, bark, leaves and wood, but only a few have ever been used on a commercial scale. The discovery of synthetic dyes late in the 19th century ended the large-scale market for natural dyes. These dyes are made from synthetic resources such as petroleum by-products, the first human-made organic aniline dye, mauveine, was discovered serendipitously by William Henry Perkin in 1856, the result of a failed attempt at the total synthesis of quinine. Other aniline dyes followed, such as fuchsine, safranine, many thousands of synthetic dyes have since been prepared. These may be natural or synthetic, other than pigmentation, they have a range of applications including organic dye lasers, optical media and camera sensors. This is the basic classification Dyes are classified according to their solubility, acid dyes are water-soluble anionic dyes that are applied to fibers such as silk, wool, nylon and modified acrylic fibers using neutral to acid dye baths. Attachment to the fiber is attributed, at least partly, to salt formation between anionic groups in the dyes and cationic groups in the fiber, acid dyes are not substantive to cellulosic fibers. Most synthetic food colors fall in this category, basic dyes are water-soluble cationic dyes that are mainly applied to acrylic fibers, but find some use for wool and silk. Usually acetic acid is added to the dye bath to help the uptake of the dye onto the fiber, basic dyes are also used in the coloration of paper
8.
Actin
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Actin is a family of globular multi-functional proteins that form microfilaments. It is found in all eukaryotic cells, where it may be present at a concentration of over 100 μM. Many of these processes are mediated by extensive and intimate interactions of actin with cellular membranes, in vertebrates, three main groups of actin isoforms, alpha, beta, and gamma have been identified. The alpha actins, found in tissues, are a major constituent of the contractile apparatus. The beta and gamma actins coexist in most cell types as components of the cytoskeleton and it is believed that the diverse range of structures formed by actin enabling it to fulfill such a large range of functions is regulated through the binding of tropomyosin along the filaments. Other enzymes or organelles such as cilia can be anchored to this scaffolding in order to control the deformation of the cell membrane. It can also produce movement either by itself or with the help of molecular motors, Actin therefore contributes to processes such as the intracellular transport of vesicles and organelles as well as muscular contraction and cellular migration. It therefore plays an important role in embryogenesis, the healing of wounds, the evolutionary origin of actin can be traced to prokaryotic cells, which have equivalent proteins. Actin homologs from prokaryotes and archaea polymerize into different helical or linear filaments consisting of one or multiple strands, however the in-strand contacts and nucleotide binding sites are preserved in prokaryotes and in archaea. Lastly, actin plays an important role in the control of gene expression, a large number of illnesses and diseases are caused by mutations in alleles of the genes that regulate the production of actin or of its associated proteins. The production of actin is also key to the process of infection by some pathogenic microorganisms, mutations in the different genes that regulate actin production in humans can cause muscular diseases, variations in the size and function of the heart as well as deafness. The make-up of the cytoskeleton is also related to the pathogenicity of bacteria and viruses. Actin was first observed experimentally in 1887 by W. D. Halliburton, in 1942, Straub developed a novel technique for extracting muscle protein that allowed him to isolate substantial amounts of relatively pure actin. Straubs method is essentially the same as used in laboratories today. Adding ATP to a mixture of both proteins causes a decrease in viscosity, the hostilities of World War II meant Szent-Gyorgyi and Straub were unable to publish the work in Western scientific journals. Actin therefore only became known in the West in 1945. Straub suggested that the transformation of ATP-bound actin to ADP-bound actin played a role in muscular contraction, in fact, this is true only in smooth muscle, and was not supported through experimentation until 2001. The amino acid sequencing of actin was completed by M. Elzinga, the crystal structure of G-actin was solved in 1990 by Kabsch and colleagues
9.
Green fluorescent protein
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The green fluorescent protein is a protein composed of 238 amino acid residues that exhibits bright green fluorescence when exposed to light in the blue to ultraviolet range. Although many other organisms have similar green fluorescent proteins, GFP traditionally refers to the protein first isolated from the jellyfish Aequorea victoria. The GFP from A. victoria has an excitation peak at a wavelength of 395 nm. Its emission peak is at 509 nm, which is in the green portion of the visible spectrum. The fluorescence quantum yield of GFP is 0.79, the GFP from the sea pansy has a single major excitation peak at 498 nm. In cell and molecular biology, the GFP gene is used as a reporter of expression. GFP can be introduced into animals or other species through transgenic techniques, and maintained in their genome, to date, GFP has been expressed in many species, including bacteria, yeasts, fungi, fish and mammals, including in human cells. Tsien, Osamu Shimomura, and Martin Chalfie were awarded the 2008 Nobel Prize in Chemistry on 10 October 2008 for their discovery and development of the green fluorescent protein. In the 1960s and 1970s, GFP, along with the separate luminescent protein aequorin, was first purified from Aequorea victoria, in A. victoria, GFP fluorescence occurs when aequorin interacts with Ca2+ ions, inducing a blue glow. Some of this luminescent energy is transferred to the GFP, shifting the overall color towards green, however, its utility as a tool for molecular biologists did not begin to be realized until 1992 when Douglas Prasher reported the cloning and nucleotide sequence of wtGFP in Gene. The funding for this project had run out, so Prasher sent cDNA samples to several labs. The lab of Martin Chalfie expressed the coding sequence of wtGFP, with the first few amino acids deleted, in cells of E. coli and C. elegans. Frederick Tsujis lab independently reported the expression of the recombinant protein one month later, remarkably, the GFP molecule folded and was fluorescent at room temperature, without the need for exogenous cofactors specific to the jellyfish. The first reported crystal structure of a GFP was that of the S65T mutant by the Remington group in Science in 1996, one month later, the Phillips group independently reported the wild-type GFP structure in Nature Biotechnology. These crystal structures provided vital background on chromophore formation and neighboring residue interactions, researchers have modified these residues by directed and random mutagenesis to produce the wide variety of GFP derivatives in use today. Due to the potential for widespread usage and the needs of researchers. The first major improvement was a point mutation reported in 1995 in Nature by Roger Tsien. This matched the spectral characteristics of commonly available FITC filter sets, a 37 °C folding efficiency point mutant to this scaffold, yielding enhanced GFP, was discovered in 1995 by the laboratories of Thastrup and Falkow
10.
Protein
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Proteins are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, a linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide, short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides, or sometimes oligopeptides. The individual amino acid residues are bonded together by peptide bonds, the sequence of amino acid residues in a protein is defined by the sequence of a gene, which is encoded in the genetic code. In general, the code specifies 20 standard amino acids, however. Sometimes proteins have non-peptide groups attached, which can be called prosthetic groups or cofactors, proteins can also work together to achieve a particular function, and they often associate to form stable protein complexes. Once formed, proteins only exist for a period of time and are then degraded and recycled by the cells machinery through the process of protein turnover. A proteins lifespan is measured in terms of its half-life and covers a wide range and they can exist for minutes or years with an average lifespan of 1–2 days in mammalian cells. Abnormal and or misfolded proteins are degraded more rapidly due to being targeted for destruction or due to being unstable. Like other biological macromolecules such as polysaccharides and nucleic acids, proteins are essential parts of organisms, many proteins are enzymes that catalyse biochemical reactions and are vital to metabolism. Proteins also have structural or mechanical functions, such as actin and myosin in muscle and the proteins in the cytoskeleton, other proteins are important in cell signaling, immune responses, cell adhesion, and the cell cycle. In animals, proteins are needed in the diet to provide the essential amino acids that cannot be synthesized, digestion breaks the proteins down for use in the metabolism. Methods commonly used to study structure and function include immunohistochemistry, site-directed mutagenesis, X-ray crystallography, nuclear magnetic resonance. Most proteins consist of linear polymers built from series of up to 20 different L-α-amino acids, all proteinogenic amino acids possess common structural features, including an α-carbon to which an amino group, a carboxyl group, and a variable side chain are bonded. Only proline differs from this structure as it contains an unusual ring to the N-end amine group. The amino acids in a chain are linked by peptide bonds. Once linked in the chain, an individual amino acid is called a residue, and the linked series of carbon, nitrogen. The peptide bond has two forms that contribute some double-bond character and inhibit rotation around its axis, so that the alpha carbons are roughly coplanar
11.
DNA
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Deoxyribonucleic acid is a molecule that carries the genetic instructions used in the growth, development, functioning and reproduction of all known living organisms and many viruses. DNA and RNA are nucleic acids, alongside proteins, lipids and complex carbohydrates, most DNA molecules consist of two biopolymer strands coiled around each other to form a double helix. The two DNA strands are termed polynucleotides since they are composed of simpler units called nucleotides. Each nucleotide is composed of one of four nitrogen-containing nucleobases—cytosine, guanine, adenine, or thymine —a sugar called deoxyribose, and a phosphate group. The nucleotides are joined to one another in a chain by covalent bonds between the sugar of one nucleotide and the phosphate of the next, resulting in an alternating sugar-phosphate backbone. The nitrogenous bases of the two polynucleotide strands are bound together, according to base pairing rules, with hydrogen bonds to make double-stranded DNA. The total amount of related DNA base pairs on Earth is estimated at 5.0 x 1037, in comparison the total mass of the biosphere has been estimated to be as much as 4 trillion tons of carbon. The DNA backbone is resistant to cleavage, and both strands of the double-stranded structure store the same biological information and this information is replicated as and when the two strands separate. A large part of DNA is non-coding, meaning that these sections do not serve as patterns for protein sequences, the two strands of DNA run in opposite directions to each other and are thus antiparallel. Attached to each sugar is one of four types of nucleobases and it is the sequence of these four nucleobases along the backbone that encodes biological information. RNA strands are created using DNA strands as a template in a process called transcription, under the genetic code, these RNA strands are translated to specify the sequence of amino acids within proteins in a process called translation. Within eukaryotic cells DNA is organized into structures called chromosomes. During cell division these chromosomes are duplicated in the process of DNA replication, eukaryotic organisms store most of their DNA inside the cell nucleus and some of their DNA in organelles, such as mitochondria or chloroplasts. In contrast prokaryotes store their DNA only in the cytoplasm, within the eukaryotic chromosomes, chromatin proteins such as histones compact and organize DNA. These compact structures guide the interactions between DNA and other proteins, helping control which parts of the DNA are transcribed, DNA was first isolated by Friedrich Miescher in 1869. DNA is used by researchers as a tool to explore physical laws and theories, such as the ergodic theorem. The unique material properties of DNA have made it an attractive molecule for material scientists and engineers interested in micro-, among notable advances in this field are DNA origami and DNA-based hybrid materials. DNA is a polymer made from repeating units called nucleotides
12.
Microbiology
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Microbiology is the study of microscopic organisms, those being unicellular, multicellular, or acellular. Microbiology encompasses numerous sub-disciplines including virology, mycology, parasitology, microbiologists traditionally relied on culture, staining, and microscopy. However, less than 1% of the present in common environments can be cultured in isolation using current means. Microbiologists often rely on extraction or detection of nucleic acid, either DNA or RNA sequences, viruses have been variably classified as organisms, as they have been considered either as very simple microorganisms or very complex molecules. As an application of microbiology, medical microbiology is often introduced with medical principles of immunology as microbiology and immunology, otherwise, microbiology, virology, and immunology as basic sciences have greatly exceeded the medical variants, applied sciences. The existence of microorganisms was hypothesized for many centuries before their actual discovery, the existence of unseen microbiological life was postulated by Jainism which is based on Mahavira’s teachings as early as 6th century BCE. Paul Dundas notes that Mahavira asserted existence of unseen microbiological creatures living in earth, water, air, in 1546, Girolamo Fracastoro proposed that epidemic diseases were caused by transferable seedlike entities that could transmit infection by direct or indirect contact, or vehicle transmission. However, early claims about the existence of microorganisms were speculative, actual observation and discovery of microbes had to await the invention of the microscope in the 17th century. In 1676, Anton van Leeuwenhoek, who lived most of his life in Delft, Holland, observed bacteria and other microorganisms using a single-lens microscope of his own design. While Van Leeuwenhoek is often cited as the first to observe microbes, Robert Hooke made the first recorded microscopic observation, of the bodies of moulds. It has, however, been suggested that a Jesuit priest called Athanasius Kircher was the first to observe micro-organisms and he was among the first to design magic lanterns for projection purposes, so he must have been well acquainted with the properties of lenses. One of his books contains a chapter in Latin, which reads in translation – Concerning the wonderful structure of things in nature, here, he wrote who would believe that vinegar and milk abound with an innumerable multitude of worms. He also noted that material is full of innumerable creeping animalcule. These observations antedate Robert Hookes Micrographia by nearly 20 years and were published some 29 years before van Leeuwenhoek saw protozoa and 37 years before he described having seen bacteria. Joseph Lister was the first person who said infectious diseases are caused by micro-organism and was first person who used phenol as disinfectant on the wounds of patients. Cohn was also the first to formulate a scheme for the classification of bacteria. Louis Pasteur and Robert Koch were contemporaries of Cohn’s and are considered to be the father of microbiology and medical microbiology. Pasteur is most famous for his series of experiments designed to disprove the widely held theory of spontaneous generation
. PMID 2456365.
