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postulation of a biosynthetic pathway.

The rate of protein synthesis is ..

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Synthesis of silk, mechanism and location, ..

Serine is the organic compound with the formula HO2CCH(NH2)CH2OH. It is one of the 20 amino acids commonly found in animal proteins. Its three letter code is ser, its one letter code is S, and its codons are AGU and AGC.[1] Only the L-stereoisomer appears in mammalian protein. It is not essential to the human diet, since it is synthesized in the body from other metabolites, including glycine. Serine was first obtained from silk protein, a particularly rich source, in 1865. Its name is derived from the Latin for silk, sericum. Serine's structure was established in 1902. The hydroxyl group attached makes it a polar amino acid.

Synthesis of silk, mechanism and location.

Aspartic acid is an α-amino acid with the chemical formula HO2CCH(NH2)CH2CO2H. The L-isomer is one of the 20 proteinogenic amino acids, i.e. the building blocks of proteins. Its three letter code is asp, its one letter code is D, and its codons are GAU and GAC.[1] It is classified as an acidic amino acid, together with glutamic acid. Aspartic acid is pervasive in biosynthesis.

Synthesis of Silk, Mechanism and Location.

Synthesis of silk, mechanism and location

As an essential amino acid, threonine is not synthesized in humans, hence we must ingest threonine or, more commonly, threonine-containing proteins. In plants and microorganisms, threonine is synthesized from aspartic acid via α-aspartyl-semialdehyde and homoserine. Homoserine undergoes O-phosphorylation; this phosphate ester undergoes hydrolysis concomitant with relocation of the OH group.[1] Enzymes involved in a typical biosynthesis of threonine include:

The SDLE Research Center was established in 2011 with funding from Ohio Third Frontier, and is dedicated to advancing the field of lifetime and degradation science. The research center activities focus on durability and degradation of environmentally exposed, long lived materials and technologies such as photovoltaics (PV), energy efficient lighting, and building envelope applications. The Center develops real-time and accelerated protocols for exposure to solar radiation and related environmental stressors to enable the evaluation of the environmental durability and lifetime of materials, components, and products. Data scientists identify statistically significant relationships using a data analytics platform (Energy-CRADLE) developed in the center. Researchers perform post-exposure optical and thermo-mechanical measurements to develop quantitative mechanistic models of degradation processes. The SDLE Research Center’s capabilities and equipment include:

enzyme kinetics studies explore the chemical mechanism of an ..

· Strong knowledge of membrane synthesis and transport mechanism through membrane

Like other amino acids, glutamine is biochemically important as a constituent of proteins. Glutamine is also crucial in nitrogen metabolism. Ammonia (formed by nitrogen fixation) is assimilated into organic compounds by converting glutamic acid to glutamine. The enzyme that accomplishes this is called glutamine synthetase. Glutamine can, hence, be used as a nitrogen donor in the biosynthesis of many compounds, including other amino acids, purines, and pyrimidines.

Experimental techniques to detect glutamate in intact cells include using a genetically-engineered nanosensor[2]. The sensor is a fusion of a glutamate-binding protein and two fluorescent proteins. When glutamate binds, the fluorescence of the sensor under ultraviolet light changes by resonance between the two fluorophores. Introduction of the nanosensor into cells enables optical detection of the glutamate concentration. Synthetic analogs of glutamic acid that can be activated by ultraviolet light have also been described[6]. This method of rapidly uncaging by photostimulation is useful for mapping the connections between neurons, and understanding synapse function.

Dr. Jon Takemoto. SBC Faculty. Current research deals with the discovery, design, synthesis, and mechanism of action of microbial natural products and their derivatives.
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  • Concerted Gene Expressions in Elicited Fibroin ..

    Protein - Wikipedia

  • Ultrastructure of the major ampullate gland of the ..

    Biosynthesis - Wikipedia

  • cob web silk from the black widow spider, Latrodectus hesperus

    Biosynthesis (also called ..

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The bulk of the synthesis of silk ..

Tyrosine cannot be completely synthesized by animals, although it can be made by hydroxylation of phenylalanine if the latter is in abundant supply. It is produced by plants and most microorganisms from prephenate, an intermediate on the shikimate pathway.

Engineering Properties of Spider Silk Fibers | SpringerLink

Tyrosine, 4-hydroxyphenylalanine, or 2-amino-3(4-hydroxyphenyl)-propanoic acid, is one of the 20 amino acids that are used by cells to synthesize proteins. It has a phenol side chain with a hydroxyl group. Upon the location of the hydroxyl group, there are three structural isomers of Tyr, namely para-Tyr (p-Tyr), meta-Tyr (m-Tyr) and ortho-Tyr (o-Tyr). Enzymatically, only the first isomer (p-Tyr) is produced from L-Phe by the Phe-hydroxylase enzyme. The other two isoforms, m-Tyr and o-Tyr can be produced as a consequence of free radical attack on Phe in states with increased oxidative stress.

(2004) Engineering Properties of Spider Silk Fibers

According to popular belief, eating tryptophan in turkey meat causes drowsiness. Turkey does contain tryptophan, which does have a documented sleep-inducing effect as it is readily converted into serotonin by the body. However, ingestion of turkey alone has not been proven to have this effect. An additional hypothetical mechanism is as follows: A large quantity of any food,[original research?] such as a Thanksgiving feast, introduces large quantities of both carbohydrates and branched-chain amino acids releasing insulin. Insulin stimulates the uptake of large neutral branched-chain amino acids (and not tryptophan) by muscle cells through the myocyte membranes. The result is an increase in the ratio of tryptophan to large neutral amino acids in the blood. This reduces competition with other amino acids for the Large Neutral Amino Acid Transporter protein for uptake of tryptophan across the blood-brain barrier into the central nervous system. Once inside the central nervous system, tryptophan is converted into serotonin by the raphe nuclei, and serotonin is further metabolised into melatonin by the pineal gland.
Alcoholic beverage consumption at holiday feasts is likely to compound the effect.[original research?]

Genetically engineered silk-elastinlike protein polymers for ..

In organisms which synthesize tryptophan, high levels of this amino acid activate a repressor protein which in turn binds to the trp operon. Binding of this repressor to its operon prevents transcription of downstream DNA which codes for enzymes involved in the biosynthesis of tryptophan. Hence high levels of tryptophan prevent additional tryptophan synthesis through a negative feedback loop. Conversely if the cell's tryptophan level drops, transcription of the operon's genes resumes. This is one example of how gene expression responds rapidly to changes in the cell's internal and external environment.

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