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Graduated as pharmacist. Feel free to contact me about anything related.

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The proteasome [1]: a crucial structure of protein degradation

The proteasome Proteins are constantly being synthesized and at the same time being degraded in each cell of our body. One of the most known mechanisms of proteolysis (= protein degradation) is the degradation done by lysosomes. However, an other important mechanism is degradation by the ubiquitin proteasome system (UPS). First of all, it is needed to understand that a cell maintains its protein concentration by a constant turn-over of proteins: when there is a lot of synthesis of a certain protein, this certain protein will also be degraded by a higher level, and vice versa. A protein that has to be degraded will be marked by a polyubiquitin chain which consists of 4 or more ubiquitinmolecules. This protein will be transported to a 26S proteasome. This structure in the cell is built by a 19S part and a 20S part. The 19S part mainly serves as a recognition and binding structure for the polyubiquitinated protein, and the 20S part will destroy the protein. Once attached to the...
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Alkynes: addition of H2 gas and Lindlar catalyst

Alkynes: addition of Hydrogen gas (H2) Performing a catalytic reduction on an alkyn will result in giving an alkane. The alkene intermediate will be formed in the process, but will immediately react into an alkane. The end result is just the formed alkane, without stacking of the alkene intermediate. The Lindlar catalyst In theory this is a "poisoned or defected" catalyst. If you use a normal catalyst you will get the above effect with your alkyne. The Lindlar catalyst contains Palladium combined with Calcium-carbonate and treated with Lead. Palladium is the actual catalyst, the calcium carbonate is the carrier of the substance and the lead is the poisonous compound. Using the Lindlar catalyst instead of another catalyst together with Hydrogen gas, will lead into forming the cis-alkene intermediate instead of the forming of the corresponding alkane. 
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Erythropoietin: definition, structure, synthesis in vivo

Definition: EPO: = erythropoietin   A glycoprotein hormon-like structure, a sialoglycoprotein, which is an important factor in the survival, growth and proliferation of erythroid precursor cells (EPC) and it improves the de novo creation, differentation and growth of red blood cells (RBC). Thus, EPO controls the erythropoiesis = production of RBC. EPC: these are cells that are located in the bone marrow, will eventually form the RBC. RBC: cells responsible for the transport and distribution of oxygen throughout the body. Structure: Built out of 165 aminoacids (AA). They are all connected and form 1 polypeptide chain.  Although, within the chain, there are 2 disulfide bonds.  Respectively on positions: Cys7-161 and Cys29-33  Cys = cystein and the numbers indicate the positions these AA are located. Cystein structure. Available  sulfide  group for bonding There are also 4 positions where there is a possibility for glycosylation  Namel...
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