Split-intein Circular Ligation Of Peptides And Proteins
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Split-intein Circular Ligation Of Peptides And Proteins
Split-intein circular ligation of peptides and proteins (SICLOPPS) is a biotechnology technique that permits the creation of cyclic peptides. These peptides are produced by ribosomal protein synthesis, followed by an intein-like event that splices the protein into a loop. By contrast with the nonribosomal peptide synthetases that produces some cyclic peptides like gramicidin S, SICLOPPS offers the advantage that the peptides' structure can be encoded by DNA in a simple manner according to the genetic code, but for this reason it imposes limitations on the types of amino acids incorporated that are comparable to those that apply to ordinary proteins. As implemented there is also some constraint on the peptide sequence of the cyclic sequence; for example, libraries may use the sequence S GXX..XX P L to increase the efficiency of circularization of the peptide. SICLOPPS is frequently used with a library of randomized DNA sequence that permits the simultaneous production and screen ...
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Biotechnology
Biotechnology is a multidisciplinary field that involves the integration of natural sciences and Engineering Science, engineering sciences in order to achieve the application of organisms and parts thereof for products and services. Specialists in the field are known as biotechnologists. The term ''biotechnology'' was first used by Károly Ereky in 1919 to refer to the production of products from raw materials with the aid of living organisms. The core principle of biotechnology involves harnessing biological systems and organisms, such as bacteria, yeast, and plants, to perform specific tasks or produce valuable substances. Biotechnology had a significant impact on many areas of society, from medicine to agriculture to environmental science. One of the key techniques used in biotechnology is genetic engineering, which allows scientists to modify the genetic makeup of organisms to achieve desired outcomes. This can involve inserting genes from one organism into another, and con ...
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Proline
Proline (symbol Pro or P) is an organic acid classed as a proteinogenic amino acid (used in the biosynthesis of proteins), although it does not contain the amino group but is rather a secondary amine. The secondary amine nitrogen is in the protonated form (NH2+) under biological conditions, while the carboxyl group is in the deprotonated −COO− form. The "side chain" from the α carbon connects to the nitrogen forming a pyrrolidine loop, classifying it as a aliphatic amino acid. It is non-essential in humans, meaning the body can synthesize it from the non-essential amino acid L-glutamate. It is encoded by all the codons starting with CC (CCU, CCC, CCA, and CCG). Proline is the only proteinogenic amino acid which is a secondary amine, as the nitrogen atom is attached both to the α-carbon and to a chain of three carbons that together form a five-membered ring. History and etymology Proline was first isolated in 1900 by Richard Willstätter who obtained the amino a ...
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Intron
An intron is any nucleotide sequence within a gene that is not expressed or operative in the final RNA product. The word ''intron'' is derived from the term ''intragenic region'', i.e., a region inside a gene."The notion of the cistron .e., gene... must be replaced by that of a transcription unit containing regions which will be lost from the mature messenger – which I suggest we call introns (for intragenic regions) – alternating with regions which will be expressed – exons." (Gilbert 1978) The term ''intron'' refers to both the DNA sequence within a gene and the corresponding RNA sequence in RNA transcripts. The non-intron sequences that become joined by this RNA processing to form the mature RNA are called exons. Introns are found in the genes of most eukaryotes and many eukaryotic viruses, and they can be located in both protein-coding genes and genes that function as RNA ( noncoding genes). There are four main types of introns: tRNA introns, group I introns, group I ...
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Exon Shuffling
Exon shuffling is a molecular mechanism for the formation of new genes. It is a process through which two or more exons from different genes can be brought together ectopically, or the same exon can be duplicated, to create a new exon-intron structure. There are different mechanisms through which exon shuffling occurs: transposon mediated exon shuffling, crossover during sexual recombination of parental genomes and illegitimate recombination. Exon shuffling follows certain splice frame rules. Introns can interrupt the reading frame of a gene by inserting a sequence between two consecutive codons (phase 0 introns), between the first and second nucleotide of a codon (phase 1 introns), or between the second and third nucleotide of a codon (phase 2 introns). Additionally exons can be classified into nine different groups based on the phase of the flanking introns (symmetrical: 0-0, 1-1, 2-2 and asymmetrical: 0–1, 0–2, 1–0, 1–2, etc.) Symmetric exons are the only ones that ...
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Combinatorial Chemistry
Combinatorial chemistry comprises chemical synthesis, chemical synthetic methods that make it possible to prepare a large number (tens to thousands or even millions) of compounds in a single process. These compound library, compound libraries can be made as mixtures, sets of individual compounds or chemical structures generated by computer software. Combinatorial chemistry can be used for the synthesis of small molecules and for peptides. Strategies that allow identification of useful components of the libraries are also part of combinatorial chemistry. The methods used in combinatorial chemistry are applied outside chemistry, too. Introduction The basic principle of combinatorial chemistry is to prepare compound library, libraries of a very large number of compounds and identify those which are useful as potential drugs or agrochemicals. This relies on high-throughput screening which is capable of assessing the output at sufficient scale. Although combinatorial chemistry has only ...
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Mechanism Of Action
In pharmacology, the term mechanism of action (MOA) refers to the specific biochemical Drug interaction, interaction through which a Medication, drug substance produces its pharmacological effect. A mechanism of action usually includes mention of the specific molecular targets to which the drug binds, such as an enzyme or receptor (biochemistry), receptor. Receptor sites have specific affinities for drugs based on the chemical structure of the drug, as well as the specific action that occurs there. Drugs that do not bind to receptors produce their corresponding therapeutic effect by simply interacting with chemical or physical properties in the body. Common examples of drugs that work in this way are antacids and laxatives. In contrast, a Mode of action, mode of action (MoA) describes functional or anatomical changes, at the cellular level, resulting from the exposure of a living organism to a substance. Importance Elucidating the mechanism of action of novel drugs and medicati ...
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Functional Complementation
Functional may refer to: * Movements in architecture: ** Functionalism (architecture) ** Form follows function * Functional group, combination of atoms within molecules * Medical conditions without currently visible organic basis: ** Functional symptom ** Functional disorder * Functional classification for roads * Functional organization * Functional training In mathematics * Functional (mathematics), a term applied to certain scalar-valued functions in mathematics and computer science ** Minnesota functionals ** Functional analysis, a branch of mathematical analysis ** Linear functional, a type of functional often simply called a functional in the context of functional analysis * Higher-order function, also called a functional, a function that takes other functions as arguments In computer science, software engineering * "Functional" (noun) may be used as a synonym for Higher-order function * (C++), a header file in the C++ Standard Library * Functional design, a paradig ...
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Orally Administered
Oral administration is a route of administration whereby a substance is taken through the mouth, swallowed, and then processed via the digestive system. This is a common route of administration for many medications. Oral administration can be easier and less painful than other routes of administration, such as injection. However, the onset of action is relatively low, and the effectiveness is reduced if it is not absorbed properly in the digestive system, or if it is broken down by digestive enzymes before it can reach the bloodstream. Some medications may cause gastrointestinal side effects, such as nausea or vomiting, when taken orally. Oral administration can also only be applied to conscious patients, and patients able to swallow. Terminology ''Per os'' (; ''P.O.'') is an adverbial phrase meaning literally from Latin "through the mouth" or "by mouth". The expression is used in medicine to describe a treatment that is taken orally (but not used ''in'' the mouth such as, fo ...
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Protease
A protease (also called a peptidase, proteinase, or proteolytic enzyme) is an enzyme that catalysis, catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. They do this by cleaving the peptide bonds within proteins by hydrolysis, a reaction where water breaks Covalent bond, bonds. Proteases are involved in numerous biological pathways, including Digestion#Protein digestion, digestion of ingested proteins, protein catabolism (breakdown of old proteins), and cell signaling. In the absence of functional accelerants, proteolysis would be very slow, taking hundreds of years. Proteases can be found in all forms of life and viruses. They have independently convergent evolution, evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Classification Based on catalytic residue Proteases can be classified into seven broad ...
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Antimicrobial Peptide
Antimicrobial peptides (AMPs), also called host defence peptides (HDPs) are part of the innate immune response found among all classes of life. Fundamental differences exist between prokaryotic and eukaryotic cells that may represent targets for antimicrobial peptides. These peptides are potent, broad spectrum antimicrobials which demonstrate potential as novel therapeutic agents. Antimicrobial peptides have been demonstrated to kill Gram negative and Gram positive bacteria, enveloped viruses, fungi and even transformed or cancerous cells. Unlike the majority of conventional antibiotics it appears that antimicrobial peptides frequently destabilize biological membranes, can form transmembrane channels, and may also have the ability to enhance immunity by functioning as immunomodulators. Structure Antimicrobial peptides are a unique and diverse group of molecules, which are divided into subgroups on the basis of their amino acid composition and structure. Antimicrobial peptides ...
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Leucine
Leucine (symbol Leu or L) is an essential amino acid that is used in the biosynthesis of proteins. Leucine is an α-amino acid, meaning it contains an α-amino group (which is in the protonated −NH3+ form under biological conditions), an α-Carboxylic acid, carboxylic acid group (which is in the deprotonated −COO− form under biological conditions), and a side chain Isobutyl, isobutyl group, making it a Chemical polarity, non-polar Aliphatic compound, aliphatic amino acid. It is Essential amino acid, essential in humans, meaning the body cannot synthesize it; it must be obtained from the diet. Human dietary sources are foods that contain protein, such as meats, dairy products, soy products, and beans and other legumes. It is genetic code, encoded by the codons UUA, UUG, CUU, CUC, CUA, and CUG. Leucine is named after the Greek language, Greek word for "white": ''λευκός'' (''leukós'', "white"), after its common appearance as a white powder, a property it shares with many ...
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Glycine
Glycine (symbol Gly or G; ) is an amino acid that has a single hydrogen atom as its side chain. It is the simplest stable amino acid. Glycine is one of the proteinogenic amino acids. It is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG). Glycine disrupts the formation of alpha-helices in secondary protein structure. Its small side chain causes it to favor random coils instead. Glycine is also an inhibitory neurotransmitter – interference with its release within the spinal cord (such as during a '' Clostridium tetani'' infection) can cause spastic paralysis due to uninhibited muscle contraction. It is the only achiral proteinogenic amino acid. It can fit into both hydrophilic and hydrophobic environments, due to its minimal side chain of only one hydrogen atom. History and etymology Glycine was discovered in 1820 by French chemist Henri Braconnot when he hydrolyzed gelatin by boiling it with sulfuric acid. He originally called it "sugar of ...
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