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Protein Synthesis -Translation and Regulation
Professor Hegner’s work focuses on individual ribosomes, which are complex molecules that use genetic information to assemble proteins. There can be several million ribosomes in a typical human cell and they are about 20 nanometres in diameter. The assembly of proteins is crucial for a healthy functioning body as all the proteins in our bodies must fold into complex shapes to do their job.
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 .
Protein Folding and Denaturation - Home | London …
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).
Denaturation may be effectively treated as an increased solubility of the unfolded form in a manner similar to that given in the treatment of the . Thus, protein aggregates and amyloid fibrils (such as are found in prion and Alzheimer's diseases) may be dissolved on cooling or under high pressure .
Protein synthesis and folding analysis on a chip
b In 1969, Cyrus Levinthal gave a that noted that a protein with N amino acids should have 102N degrees of freedom Thus a small protein (e.g. 150 amino acids) would have 10300 degrees of freedom. There is not enough time in the Universe to try each of these combinations and yet the protein is folded within a second. This is known as Levinthal's paradox. 
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.
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Protein synthesis, folding, modification, and secretion …
At ambient temperature, the entropies of hydration of both non-polar and polar groups are negative  indicating that both create order in the aqueous environment. However, these entropies differ with respect to how they change with increasing temperature. The entropy of hydration of non-polar groups increases through zero with increasing temperature, indicating that they are less able to order the water at higher temperatures and may, indeed, contribute to its disorder by interfering with the extent of the hydrogen-bonded network and allowing an easier molecular rotation of water. Also, there is an entropy gain from the greater freedom of the non-polar groups when the protein is unfolded. In contrast, the entropy of hydration of polar groups decreases, becoming more negative with increasing temperature, as they are able to create ordered hydration shells even from the more disordered water that exists at higher temperatures. A consequence is that the water is more ordered around hydrophilic groups, compared with just water, as the temperature is raised and that this hydrophilic hydration has negative heat capacity .
Protein synthesis and folding | …
A team of international researchers led by Professor in Physics at Trinity, Martin Hegner, an Investigator in CRANN, has for the first time observed how proteins fold while being produced in real time.
Protein Folding in the Neuron and the Mind | Jon Lieff, M.D.
In contrast, the enthalpy of transfer of non-polar groups from the protein interior into water is negative below about 25 °C and positive above . At lower temperatures, non-polar groups enhance pre-existing order such as the clathrate-related structure , discussed , generating enthalpy but this effect is lost with increasing temperature, as any pre-existing order is also lost. At higher temperatures, the creation of these clathrate structures requires an enthalpic input. Thus, there is an overall positive enthalpy of unfolding at higher temperatures. An equivalent but alternative way of describing this process is that at lower temperatures the clathrate-type structure optimizes its multiple molecular interactions whereas at higher temperatures such favorable structuring is no longer available.
Meeting Theme: Protein Synthesis and Degradation - …
The work has significant implications for understanding protein synthesis generally, and particularly in neurogenerative diseases such as Alzheimer’s and Parkinson’s. The team's findings have just been published in the prestigious journal Proceedings of the National Academy of Sciences. The article can be read .
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