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Diagram showing how a protein is produced

N2 - A form of associative plasticity in Aplysia, activity-dependent neuromodulation, involves the convergence of neuronal activity and the effects of a modulatory transmitter. To investigate the role of protein synthesis in associative plasticity, we examined the effects of a biochemical analogue of activity-dependent neuromodulation on the level of incorporation of labeled amino acid into proteins. To mimic associative training, abdominal ganglia were exposed to paired treatments of a depolarizing agent, elevated potassium, and a modulatory transmitter, serotonin. The effects of elevated potassium and serotonin applied alone were also examined. At least two proteins (nos. 9 and 17) were affected in a nonadditive way by the paired procedure. Incorporation of label into protein 9 was increased by the paired procedure but was not affected by either elevated potassium or serotonin. Incorporation of label into protein 17 was significantly affected by elevated potassium or serotonin, but the effect of the paired procedure was significantly less than the summed effects of elevated potassium and serotonin applied alone. These results indicate that changes in protein synthesis may be important in the induction of associative plasticities. Amino acid sequences of two peptides derived from protein 9 were obtained. Then, a partial cDNA clone for protein 9 was obtained by performing PCR with degenerate primers corresponding to portions of the sequences of the two peptides. The sequence of protein 9 is related to sequences previously reported for a family of genes comprising the stringent starvation protein of Escherichia coli, auxin-induced proteins of plants, and glutathione S- transferases of a number of organisms.

AB - A form of associative plasticity in Aplysia, activity-dependent neuromodulation, involves the convergence of neuronal activity and the effects of a modulatory transmitter. To investigate the role of protein synthesis in associative plasticity, we examined the effects of a biochemical analogue of activity-dependent neuromodulation on the level of incorporation of labeled amino acid into proteins. To mimic associative training, abdominal ganglia were exposed to paired treatments of a depolarizing agent, elevated potassium, and a modulatory transmitter, serotonin. The effects of elevated potassium and serotonin applied alone were also examined. At least two proteins (nos. 9 and 17) were affected in a nonadditive way by the paired procedure. Incorporation of label into protein 9 was increased by the paired procedure but was not affected by either elevated potassium or serotonin. Incorporation of label into protein 17 was significantly affected by elevated potassium or serotonin, but the effect of the paired procedure was significantly less than the summed effects of elevated potassium and serotonin applied alone. These results indicate that changes in protein synthesis may be important in the induction of associative plasticities. Amino acid sequences of two peptides derived from protein 9 were obtained. Then, a partial cDNA clone for protein 9 was obtained by performing PCR with degenerate primers corresponding to portions of the sequences of the two peptides. The sequence of protein 9 is related to sequences previously reported for a family of genes comprising the stringent starvation protein of Escherichia coli, auxin-induced proteins of plants, and glutathione S- transferases of a number of organisms.

Since many of the proteins made are enzymes, genes control the cell's internal chemistry.

What Is Protein Synthesis - Protein Synthesis

Overall, protein stability depends on the balance between these enthalpic and entropic changes. For globular proteins, the ΔG of unfolding has a maximum 10-30 °C, decreasing both colder and hotter through zero with the thermodynamic consequences of both cold and heat denaturation. The hydration of the internal non-polar groups is mainly responsible for cold denaturation as their energy of hydration is greatest when cold. Thus, it is the increased natural structuring of water at lower temperatures that causes cold destabilization of proteins in solution (that is, the entropic cost of denaturation, due to the structuring of the water molecules around the exposed groups, is reduced) []. An equivalent alternative view is that the increase as the temperature is raised from a low value, such that the extended polypeptide chain, present at very low temperatures, folds up to produce an active globular protein so releasing water molecules to the bulk environment.

Proteins may form crystals when slowly from an aqueous solution (e.g. of ammonium sulfate). Slow precipitation is required to produce small numbers of larger crystals rather than very large numbers of small crystals. Crystals of undenatured proteins for structural analysis are best formed with water molecules retained within the crystal lattice. Crystallization of native proteins appears to have a three-step mechanism involving nucleation, in which mesoscopic metastable protein clusters of dense liquid serve as precursors to the ordered crystal nuclei followed by crystal growth []. This process seems to involve an and fits nicely with the , where the crystallization takes place within the dense phase.

Protein synthesis - Biology-Online Dictionary

The word 'Prions' (pronounced Pree-Ons) is short for proteinaceous infection particles and has been found to be small mutated protein molecules related to infectious diseases like that of mad cow disease and scrapies in animals and including kuru and Creutzfeldt-Jakob diseases in humans. The term prions itself was first coined in 1982 by Stanley B. Prusiner an American scientist whom for two decades struggled to convince his peers that certain proteins were possibly responsible for various unusual brain diseases, which in medical terms are called spongiform encephalopathies. Prusiner was later in 1997 presented with the Nobel prize in medicine. Prion proteins are as stated in their name protein molecules and as such have no nucleic acid genetic information. Instead, the proteins are made up of amino acids, which due to a defect subsequently direct the prion protein to fold into fibrils in a dysfunctional manner which then aggregate. This abnormal folding occurs when the normal mainly-helical PrPc protein refolds to form an abnormal PrPsc protein with a substantial β-sheet substructure (see below right).

Although the native state of a protein resides at a minimum on the potential energy surface, there is no reason to suppose that this structure is the global minimum free energy structure as its folding route is a guided, rather than random, process. It is clear that other structures with lower minima exist, such as those often irreversibly produced on denaturation, for example on heating followed by cooling, which utilizes other intermolecular interactions [].

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Protein Synthesis -Translation and Regulation


quiz protein synthesis - Biology Junction

Similar effects may be seen on the activity of enzymes with hydration [] although complete hydration is unnecessary for some activity to be evident. Under physiological conditions inside cells, the water is known to be more ordered (see ). Such water promotes both the folding rate and stability of the protein [] even further.

What is the role of messenger RNA and ribosomes in protein synthesis

Eventually, the ribosome will come to a stop codon. The three stop codons don't code for any amino acids, and so the process comes to a halt. The protein chain produced up to that point is then released from the ribosome, and then folds itself up into its secondary and tertiary structures.

Protein synthesis :: DNA from the Beginning

Each gene acts as a code, or set of instructions, for making a particular protein. Some of these proteins control the cell's internal chemistry. They tell the cell what to do, give the organism its characteristics, and determine the way its body works.

Protein Synthesis Flashcards | Quizlet

After translation, the protein passes into the channels of the rough endoplasmic reticulum (ER) for transportation. The protein is then passed from the rough ER to the Golgi apparatus inside tiny fluid-filled sacs, called vesicles. The Golgi apparatus is a system of , which are responsible for the modification, processing, and packaging of the proteins. The protein may have a carbohydrate added, to form a glycoprotein. The Golgi apparatus packages the protein in a secretory vesicle, which fuses with the cell membrane and releases the protein from the cell.

Diagram showing how a protein is produced.

Each and every protein when activated folds in a specific way; prion proteins are no different. When an abnormal PrPsc protein folds, it folds in an unusual way which adversely affects the neuronal cells. The PrPsc protein then attaches to other healthy PrPc proteins, building a template that changes the normal conformation of the healthy prion protein to that of the disease-causing highly stable proteins [].

We can regard protein synthesis as a ..

A form of associative plasticity in Aplysia, activity-dependent neuromodulation, involves the convergence of neuronal activity and the effects of a modulatory transmitter. To investigate the role of protein synthesis in associative plasticity, we examined the effects of a biochemical analogue of activity-dependent neuromodulation on the level of incorporation of labeled amino acid into proteins. To mimic associative training, abdominal ganglia were exposed to paired treatments of a depolarizing agent, elevated potassium, and a modulatory transmitter, serotonin. The effects of elevated potassium and serotonin applied alone were also examined. At least two proteins (nos. 9 and 17) were affected in a nonadditive way by the paired procedure. Incorporation of label into protein 9 was increased by the paired procedure but was not affected by either elevated potassium or serotonin. Incorporation of label into protein 17 was significantly affected by elevated potassium or serotonin, but the effect of the paired procedure was significantly less than the summed effects of elevated potassium and serotonin applied alone. These results indicate that changes in protein synthesis may be important in the induction of associative plasticities. Amino acid sequences of two peptides derived from protein 9 were obtained. Then, a partial cDNA clone for protein 9 was obtained by performing PCR with degenerate primers corresponding to portions of the sequences of the two peptides. The sequence of protein 9 is related to sequences previously reported for a family of genes comprising the stringent starvation protein of Escherichia coli, auxin-induced proteins of plants, and glutathione S- transferases of a number of organisms.

Continued Protein Synthesis at Low [ATP] and [GTP] …

Translating the code into an actual protein chain is complicated by the fact that individual amino acids won't interact with the messenger RNA chain. The amino acids have to be carried to the messenger RNA by another type of RNA known as transfer RNA - abbreviated to tRNA (as opposed to mRNA for messenger RNA).

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