Tyrocidine H-bonding
Tyrocidine is a mixture of cyclic decapeptides produced by the bacteria ''Bacillus brevis'' found in soil. It can be composed of 4 different amino acid sequences, giving tyrocidine A–D (See figure 1). Tyrocidine is the major constituent of tyrothricin, which also contains gramicidin.Pubchem: Tyrocidine and Tyrothricin. Tyrocidine was the first commercially available antibiotic, but has been found to be toxic toward human blood and reproductive cells. The function of tyrocidine within its host ''B. brevis'' is thought to be regulation of sporulation. Tyrocidines A, B, and C are cyclic decapeptides. The biosynthesis of tyrocidine involves three enzymes. Parts of its sequence are identical to gramicidin S. History In 1939, the American microbiologist René Dubos discovered the soil microbe ''Bacillus brevis''. He observed the ability of the microbe to decompose the capsule of pneumococcus bacterium, rendering it harmless. From the soil microbe ''B. brevis'', he isolated t ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Bacillus Brevis
''Brevibacillus brevis'' (formerly known as ''Bacillus brevis'') is a Gram-positive, aerobic, motile, spore-forming, rod-shaped bacterium commonly found in soil, air, water, and decaying matter. It is rarely associated with infectious diseases. The antibiotics gramicidin and tyrocidine were first isolated from it.Abedon, Stephen. "Bacteria Binomials." 26 Apr 1998. Ohio State University. 17 Jun 2006 . ''Brevibacillus brevis'' is catalase positive, amylase negative, casein negative, gelatinase positive, and indole negative; most strains are citrate users. Some strains are capable of oxidizing carbon monoxide Carbon monoxide (chemical formula CO) is a colorless, poisonous, odorless, tasteless, flammable gas that is slightly less dense than air. Carbon monoxide consists of one carbon atom and one oxygen atom connected by a triple bond. It is the simple ... aerobically. Optimal growth occurs at 35 °C to 55 °C. References Paenibacillaceae Bacteria described in ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Epimerization
In stereochemistry, an epimer is one of a pair of diastereomers. The two epimers have opposite configuration at only one stereogenic center out of at least two. All other stereogenic centers in the molecules are the same in each. Epimerization is the interconversion of one epimer to the other epimer. Doxorubicin and epirubicin are two epimers that are used as drugs. Examples The stereoisomers β-D- glucopyranose and β-D- mannopyranose are epimers because they differ only in the stereochemistry at the C-2 position. The hydroxy group in β-D-glucopyranose is equatorial (in the "plane" of the ring), while in β-D-mannopyranose the C-2 hydroxy group is axial (up from the "plane" of the ring). These two molecules are epimers but, because they are not mirror images of each other, are not enantiomers. (Enantiomers have the same name, but differ in D and L classification.) They are also not sugar anomers, since it is not the anomeric carbon involved in the stereochemistry. Simila ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Solid Phase Peptide Synthesis
In organic chemistry, peptide synthesis is the production of peptides, compounds where multiple amino acids are linked via amide bonds, also known as peptide bonds. Peptides are chemically synthesized by the condensation reaction of the carboxyl group of one amino acid to the amino group of another. Protecting group strategies are usually necessary to prevent undesirable side reactions with the various amino acid side chains. Chemical peptide synthesis most commonly starts at the carboxyl end of the peptide (C-terminus), and proceeds toward the amino-terminus ( N-terminus). Protein biosynthesis (long peptides) in living organisms occurs in the opposite direction. The chemical synthesis of peptides can be carried out using classical solution-phase techniques, although these have been replaced in most research and development settings by solid-phase methods (see below). Solution-phase synthesis retains its usefulness in large-scale production of peptides for industrial purposes ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Polyethylene Glycol
Polyethylene glycol (PEG; ) is a polyether compound derived from petroleum with many applications, from industrial manufacturing to medicine. PEG is also known as polyethylene oxide (PEO) or polyoxyethylene (POE), depending on its molecular weight. The structure of PEG is commonly expressed as H−(O−CH2−CH2)n−OH. Uses Medical uses * Pharmaceutical-grade PEG is used as an excipient in many pharmaceutical products, in oral, topical, and parenteral dosage forms. * PEG is the basis of a number of laxatives (as ''MiraLax''). Whole bowel irrigation with polyethylene glycol and added electrolytes is used for bowel preparation before surgery or colonoscopy. * PEG is used in medicines for treating disimpaction and maintenance therapy for children with constipation. * When attached to various protein medications or drug carriers, polyethylene glycol of suitable length slows down their clearance from the blood. * The possibility that PEG could be used to fuse axons is being ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Alanine Scan
In molecular biology, alanine scanning is a site-directed mutagenesis technique used to determine the contribution of a specific residue to the stability or function of a given protein. Alanine is used because of its non-bulky, chemically inert, methyl functional group that nevertheless mimics the secondary structure preferences that many of the other amino acids possess. Sometimes bulky amino acids such as valine or leucine are used in cases where conservation of the size of mutated residues is needed. This technique can also be used to determine whether the side chain of a specific residue plays a significant role in bioactivity. This is usually accomplished by site-directed mutagenesis or randomly by creating a PCR library. Furthermore, computational methods to estimate thermodynamic parameters based on theoretical alanine substitutions have been developed. This technique is rapid, because many side chains are analyzed simultaneously and the need for protein purification and ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Leaving Group
In chemistry, a leaving group is defined by the IUPAC as an atom or group of atoms that detaches from the main or residual part of a substrate during a reaction or elementary step of a reaction. However, in common usage, the term is often limited to a fragment that departs with a pair of electrons in heterolytic bond cleavage. In this usage, a leaving group is a less formal but more commonly used synonym of the term '' nucleofuge''. In this context, leaving groups are generally anions or neutral species, departing from a neutral or cationic substrates, respectively, though in rare cases, cations leaving from a dicationic substrate are also known. A species' ability to serve as a leaving group depends on its ability to stabilize the additional electron density that results from bond heterolysis. Common anionic leaving groups are halides such as Cl−, Br−, and I−, and sulfonate esters such as tosylate (TsO−), while water (H2O), alcohols (HOR), and amines (R3N) are common neutr ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Tyrocidine H-bonding
Tyrocidine is a mixture of cyclic decapeptides produced by the bacteria ''Bacillus brevis'' found in soil. It can be composed of 4 different amino acid sequences, giving tyrocidine A–D (See figure 1). Tyrocidine is the major constituent of tyrothricin, which also contains gramicidin.Pubchem: Tyrocidine and Tyrothricin. Tyrocidine was the first commercially available antibiotic, but has been found to be toxic toward human blood and reproductive cells. The function of tyrocidine within its host ''B. brevis'' is thought to be regulation of sporulation. Tyrocidines A, B, and C are cyclic decapeptides. The biosynthesis of tyrocidine involves three enzymes. Parts of its sequence are identical to gramicidin S. History In 1939, the American microbiologist René Dubos discovered the soil microbe ''Bacillus brevis''. He observed the ability of the microbe to decompose the capsule of pneumococcus bacterium, rendering it harmless. From the soil microbe ''B. brevis'', he isolated t ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Tyrocidine Cyclization
Tyrocidine is a mixture of cyclic decapeptides produced by the bacteria ''Bacillus brevis'' found in soil. It can be composed of 4 different amino acid sequences, giving tyrocidine A–D (See figure 1). Tyrocidine is the major constituent of tyrothricin, which also contains gramicidin.Pubchem: Tyrocidine and Tyrothricin. Tyrocidine was the first commercially available antibiotic, but has been found to be toxic toward human blood and reproductive cells. The function of tyrocidine within its host ''B. brevis'' is thought to be regulation of sporulation. Tyrocidines A, B, and C are cyclic decapeptides. The biosynthesis of tyrocidine involves three enzymes. Parts of its sequence are identical to gramicidin S. History In 1939, the American microbiologist René Dubos discovered the soil microbe ''Bacillus brevis''. He observed the ability of the microbe to decompose the capsule of pneumococcus bacterium, rendering it harmless. From the soil microbe ''B. brevis'', he isolated t ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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D-amino Acid
D-Amino acids are amino acids where the stereogenic carbon alpha to the amino group has the D-configuration. For most naturally-occurring amino acids, this carbon has the L-configuration. D-Amino acids are occasionally found in nature as residues in proteins. They are formed from ribosomally-derived D-amino acid residues. Amino acids, as components of peptides, peptide hormones, structural and immune proteins, are the most important bioregulators involved in all life processes along with nucleic acids, carbohydrates and lipids. "Environmental D-amino acids are thought to be derived from organic diagenesis such as racemization and release from bacterial cell walls and even from microbial production." Discovery Their discovery was in the 1950s. "Auclair and Patton (1950) first reported their presence in the blood of insects and mollusks" Furthermore, they also have been identified in various mammalian tissues. The two major types of D-amino acids synthesized in and by mamm ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Adenosine Monophosphate
Adenosine monophosphate (AMP), also known as 5'-adenylic acid, is a nucleotide. AMP consists of a phosphate group, the sugar ribose, and the nucleobase adenine; it is an ester of phosphoric acid and the nucleoside adenosine. As a substituent it takes the form of the prefix adenylyl-. AMP plays an important role in many cellular metabolic processes, being interconverted to Adenosine diphosphate, ADP and/or Adenosine triphosphate, ATP. AMP is also a component in the synthesis of RNA. AMP is present in all known forms of life. Production and degradation AMP does not have the high energy phosphoanhydride bond associated with ADP and ATP. AMP can be produced from Adenosine diphosphate, ADP: : 2 ADP → ATP + AMP Or AMP may be produced by the hydrolysis of one high energy phosphate bond of ADP: : ADP + H2O → AMP + phosphate, Pi AMP can also be formed by hydrolysis of Adenosine triphosphate, ATP into AMP and pyrophosphate: : ATP + H2O → AMP + pyrophosphate, PPi When RNA i ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Phosphopantetheine
Phosphopantetheine, also known as 4'-phosphopantetheine, is a prosthetic group of several acyl carrier proteins including the acyl carrier proteins (ACP) of fatty acid synthases, ACPs of polyketide synthases, the peptidyl carrier proteins (PCP), as well as aryl carrier proteins (ArCP) of nonribosomal peptide synthetases (NRPS). It is also present in formyltetrahydrofolate dehydrogenase. Subsequent to the expression of the ''apo'' acyl carrier protein, 4'-phosphopantetheine moiety is attached to a serine residue. The coupling involves formation of a phosphodiester linkage. This coupling is mediated by acyl carrier protein synthase (ACPS), a 4'-phosphopantetheinyl transferase. Phosphopantetheine prosthetic group covalently links to the acyl group via a high energy thioester bond. The flexibility and length of the phosphopantetheine chain (approximately 2 nm) allows the covalently tethered intermediates to access spatially distinct enzyme-active sites. This accessibility increa ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Adenosine Triphosphate
Adenosine triphosphate (ATP) is an organic compound that provides energy to drive many processes in living cells, such as muscle contraction, nerve impulse propagation, condensate dissolution, and chemical synthesis. Found in all known forms of life, ATP is often referred to as the "molecular unit of currency" of intracellular energy transfer. When consumed in metabolic processes, it converts either to adenosine diphosphate (ADP) or to adenosine monophosphate (AMP). Other processes regenerate ATP. The human body recycles its own body weight equivalent in ATP each day. It is also a precursor to DNA and RNA, and is used as a coenzyme. From the perspective of biochemistry, ATP is classified as a nucleoside triphosphate, which indicates that it consists of three components: a nitrogenous base (adenine), the sugar ribose, and the Polyphosphate, triphosphate. Structure ATP consists of an adenine attached by the 9-nitrogen atom to the 1′ carbon atom of a sugar (ribose), which i ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |