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Halobacterium Salinarum
''Halobacterium salinarum'', formerly known as ''Halobacterium cutirubrum'' or ''Halobacterium halobium'', is an extremely halophile, halophilic ocean, marine obligate aerobic archaeon. Despite its name, this is not a bacteria, bacterium, but a member of the domain Archaea. It is found in salted fish, Hide (skin), hides, Hypersaline lake, hypersaline lakes, and salterns. As these salterns reach the minimum salinity limits for extreme halophiles, their waters become purple or reddish color due to the high densities of halophilic Archaea. ''H. salinarum'' has also been found in high-salt food such as salt pork, marine fish, and sausages. The ability of ''H. salinarum'' to live at such high salt concentrations has led to its classification as an extremophile. Cell morphology and metabolism Halobacteria are single-celled, rod-shaped microorganisms that are among the most ancient forms of life and appeared on Earth billions of years ago. The membrane consists of a single lipid bilaye ...
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Archaea
Archaea ( ) is a Domain (biology), domain of organisms. Traditionally, Archaea only included its Prokaryote, prokaryotic members, but this has since been found to be paraphyletic, as eukaryotes are known to have evolved from archaea. Even though the domain Archaea Cladistics, cladistically includes eukaryotes, the term "archaea" (: archaeon , from the Greek "ἀρχαῖον", which means ancient) in English still generally refers specifically to prokaryotic members of Archaea. Archaea were initially Taxonomy (biology), classified as bacteria, receiving the name archaebacteria (, in the Archaebacteria Kingdom (biology), kingdom), but this term has fallen out of use. Archaeal cells have unique properties separating them from Bacteria and Eukaryote, Eukaryota. Archaea are further divided into multiple recognized phylum, phyla. Classification is difficult because most have not been Isolation (microbiology), isolated in a laboratory and have been detected only by their Gene, gene s ...
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S-layer
An S-layer (surface layer) is a part of the cell envelope found in almost all archaea, as well as in many types of bacteria. The S-layers of both archaea and bacteria consists of a Monolayer, monomolecular layer composed of only one (or, in a few cases, two) identical proteins or glycoproteins. This structure is built via self-assembly and encloses the whole cell surface. Thus, the S-layer protein can represent up to 15% of the whole protein content of a cell. S-layer proteins are poorly conserved or not conserved at all, and can differ markedly even between related species. Depending on species, the S-layers have a thickness between 5 and 25 nm and possess identical pores 2–8 nm in diameter. The terminology "S-layer" was used the first time in 1976. The general use was accepted at the "First International Workshop on Crystalline Bacterial Cell Surface Layers, Vienna (Austria)" in 1984, and in the year 1987 S-layers were defined at the European Molecular Biology Organiz ...
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Protein Precipitation
Protein precipitation is widely used in downstream processing of biological products in order to concentrate proteins and purify them from various contaminants. For example, in the biotechnology industry protein precipitation is used to eliminate contaminants commonly contained in blood. The underlying mechanism of precipitation is to alter the solvation potential of the solvent, more specifically, by lowering the solubility of the solute by addition of a reagent. General principles The solubility of proteins in aqueous buffers depends on the distribution of hydrophilic and hydrophobic amino acid residues on the protein's surface. Hydrophobic residues predominantly occur in the globular protein core, but some exist in patches on the surface. Proteins that have high hydrophobic amino acid content on the surface have low solubility in an aqueous solvent. Charged and polar surface residues interact with ionic groups in the solvent and increase the solubility of a protein. Knowledg ...
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Active Transport
In cellular biology, active transport is the movement of molecules or ions across a cell membrane from a region of lower concentration to a region of higher concentration—against the concentration gradient. Active transport requires cellular energy to achieve this movement. There are two types of active transport: primary active transport that uses adenosine triphosphate (ATP), and secondary active transport that uses an electrochemical gradient. This process is in contrast to passive transport, which allows molecules or ions to move down their concentration gradient, from an area of high concentration to an area of low concentration, with energy. Active transport is essential for various physiological processes, such as nutrient uptake, hormone secretion, and nig impulse transmission. For example, the sodium-potassium pump uses ATP to pump sodium ions out of the cell and potassium ions into the cell, maintaining a concentration gradient essential for cellular function. A ...
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Diffusion Equilibrium
Molecular diffusion is the motion of atoms, molecules, or other particles of a gas or liquid at temperatures above absolute zero. The rate of this movement is a function of temperature, viscosity of the fluid, size and density (or their product, mass) of the particles. This type of diffusion explains the net flux of molecules from a region of higher concentration to one of lower concentration. Once the concentrations are equal the molecules continue to move, but since there is no concentration gradient the process of molecular diffusion has ceased and is instead governed by the process of self-diffusion, originating from the random motion of the molecules. The result of diffusion is a gradual mixing of material such that the distribution of molecules is uniform. Since the molecules are still in motion, but an equilibrium has been established, the result of molecular diffusion is called a "dynamic equilibrium". In a Phase (matter), phase with uniform temperature, absent external n ...
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Potassium Chloride
Potassium chloride (KCl, or potassium salt) is a metal halide salt composed of potassium and chlorine. It is odorless and has a white or colorless vitreous crystal appearance. The solid dissolves readily in water, and its solutions have a salt-like taste. Potassium chloride can be obtained from ancient dried lake deposits. KCl is used as a salt substitute for table salt (NaCl), a fertilizer, as a medication, in scientific applications, in domestic water softeners (as a substitute for sodium chloride salt), as a feedstock, and in food processing, where it may be known as E number additive E508. It occurs naturally as the mineral sylvite, which is named after salt's historical designations ''sal degistivum Sylvii'' and ''sal febrifugum Sylvii'', and in combination with sodium chloride as sylvinite. Uses Fertilizer The majority of the potassium chloride produced is used for making fertilizer, called potash, since the growth of many plants is limited by potassium availabil ...
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Compatible Solutes
Osmoprotectants or compatible solutes are small organic molecules with neutral charge and low toxicity at high concentrations that act as osmolytes and help organisms to survive in extreme osmotic stress. Osmoprotectants can be placed in three chemical classes: betaines and associated molecules, sugars and polyols, and amino acids. These molecules accumulate in cells and balance the osmotic difference between the cell's surroundings and the cytosol. In plants, their accumulation can increase survival during stresses such as drought. In extreme cases, such as in bdelloid rotifers, tardigrades, brine shrimp, and nematodes, these molecules can allow cells to survive being completely dried out and let them enter a state of suspended animation called cryptobiosis. Intracellular osmoprotectant concentrations are regulated in response to environmental conditions such as osmolarity and temperature via regulation of specific transcription factors and transporters. They have been shown to ...
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Transcription Factor
In molecular biology, a transcription factor (TF) (or sequence-specific DNA-binding factor) is a protein that controls the rate of transcription (genetics), transcription of genetics, genetic information from DNA to messenger RNA, by binding to a specific DNA sequence. The function of TFs is to regulate—turn on and off—genes in order to make sure that they are Gene expression, expressed in the desired Cell (biology), cells at the right time and in the right amount throughout the life of the cell and the organism. Groups of TFs function in a coordinated fashion to direct cell division, cell growth, and cell death throughout life; cell migration and organization (body plan) during embryonic development; and intermittently in response to signals from outside the cell, such as a hormone. There are approximately 1600 TFs in the human genome. Transcription factors are members of the proteome as well as regulome. TFs work alone or with other proteins in a complex, by promoting (a ...
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Gluconeogenesis
Gluconeogenesis (GNG) is a metabolic pathway that results in the biosynthesis of glucose from certain non-carbohydrate carbon substrates. It is a ubiquitous process, present in plants, animals, fungi, bacteria, and other microorganisms. In vertebrates, gluconeogenesis occurs mainly in the liver and, to a lesser extent, in the cortex of the kidneys. It is one of two primary mechanisms – the other being degradation of glycogen ( glycogenolysis) – used by humans and many other animals to maintain blood sugar levels, avoiding low levels (hypoglycemia). In ruminants, because dietary carbohydrates tend to be metabolized by rumen organisms, gluconeogenesis occurs regardless of fasting, low-carbohydrate diets, exercise, etc. In many other animals, the process occurs during periods of fasting, starvation, low-carbohydrate diets, or intense exercise. In humans, substrates for gluconeogenesis may come from any non-carbohydrate sources that can be converted to pyruvate or inter ...
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Aspartate
Aspartic acid (symbol Asp or D; the ionic form is known as aspartate), is an α-amino acid that is used in the biosynthesis of proteins. The L-isomer of aspartic acid is one of the 22 proteinogenic amino acids, i.e., the building blocks of proteins. D-aspartic acid is one of two D-amino acids commonly found in mammals. Apart from a few rare exceptions, D-aspartic acid is not used for protein synthesis but is incorporated into some peptides and plays a role as a neurotransmitter/ neuromodulator. Like all other amino acids, aspartic acid contains an amino group and a carboxylic acid. Its α-amino group is in the protonated –NH form under physiological conditions, while its α-carboxylic acid group is deprotonated −COO− under physiological conditions. Aspartic acid has an acidic side chain (CH2COOH) which reacts with other amino acids, enzymes and proteins in the body. Under physiological conditions (pH 7.4) in proteins the side chain usually occurs as the negatively charged as ...
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Arginine
Arginine is the amino acid with the formula (H2N)(HN)CN(H)(CH2)3CH(NH2)CO2H. The molecule features a guanidinium, guanidino group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated (−CO2−) and both the amino and guanidino groups are protonated, resulting in a cation. Only the -arginine (symbol Arg or R) enantiomer is found naturally. Arg residues are common components of proteins. It is Genetic code, encoded by the DNA codon table, codons CGU, CGC, CGA, CGG, AGA, and AGG. The guanidine group in arginine is the Precursor (chemistry), precursor for the biosynthesis of nitric oxide. Like all amino acids, it is a white, water-soluble solid. The one-letter symbol R was assigned to arginine for its phonetic similarity. History Arginine was first isolated in 1886 from Lupinus luteus, yellow lupin seedlings by the German chemist Ernst Schulze (chemist), Ernst Schulze and his assistant Ernst Steiger. He named it from the Greek ''árg ...
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Amino Acid
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. Only these 22 appear in the genetic code of life. Amino acids can be classified according to the locations of the core structural functional groups ( alpha- , beta- , gamma- amino acids, etc.); other categories relate to polarity, ionization, and side-chain group type ( aliphatic, acyclic, aromatic, polar, etc.). In the form of proteins, amino-acid '' residues'' form the second-largest component (water being the largest) of human muscles and other tissues. Beyond their role as residues in proteins, amino acids participate in a number of processes such as neurotransmitter transport and biosynthesis. It is thought that they played a key role in enabling life on Earth and its emergence. Amino acids are formally named by the IUPAC- IUBMB Joint Commi ...
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