Find an interesting biochemistry website and put its link in this entry and describe briefly what is found there.

http://www.brookscole.com/chemistry_d/templates/student_resources/shared_resources/animations/protein_synthesis/protein_synthesis.html
This is a link to the animation of the protein synthesis. It is basically explaining the production of the protein with some pictures to accompany it and towards the end there’ll be review. This can be helpful for those who want to understand how the protein is processes.

Here’s a brief introduction: Protein synthesis is also called translation. It is occurring in the ribosome located in the mitochondria and chloroplast. In the Eukaryotic cell, the ribosome is usually attaches to the endoplasmic reticulum. While in the prokaryotic cell, there’s no endoplasmic reticulum, thus it’s capable to move around more easily. The proteins synthesize in three different processes. The first stage is called initiation; follow by elongation and lastly termination. Initiation is the production of ribosomal complex. Elongation is the process of amino acid forming polypeptide chain. Termination occurs when the protein left ribosome.

What knowledge have you connected with past knowledge?

From the past to present, I am learning each day. All the topics covered in class, I was familiar with before. I learned that proteins are composed of four structural components. These structures included Primary structure consisted of basic order sequences of amino acid, secondary structure composed of amino acid arranged in beta sheet and alpha helix, tertiary was the folding of the structure in 3D shape and quaternary consisted of subunits, which were dimmers, trimers and tetramers. Alpha helix had a hydrogen bond that made it stable and the side chains were found on the outer parts of the helix. If the helix got larger it couldn’t arrange in shape due to the bulky side groups. Beta pleaded sheet consisted of intrachain and interchain. Alpha helix and beta sheet could merge to create a supersecondary structure (motif). Myoglobin was an example of tertiary structure and hemoglobin was an example of quarternary structure.

I also learned that most enzymes were considered protein but only some proteins were considered enzymes. Enzymes were highly specific which catalyzed only on certain enzymes. When enzymes were being catalyzed, their activation energy would lower and their rate of reaction would increase. Their transition state was much more stable than the uncatalyzed enzymes. The rate of a chemical reaction of the enzymes would increase if the temperature increased. Enzymes would denature if the rate of the biochemical reaction along with the temperature reached their limit.

Find a protein using PDB explorer-decribe your protein, including what disease state or other real-world application it has.

The YIxR protein was part of the streptococcus pneumonia and its purpose was not yet known. It derived from a small group of protein called alpha-beta plait super family that had motif GRGA. Their protein was not the same as other protein; moreover, their structure was similar to a double layer alpha/beta sandwich. The protein structure was identified through semi-automated. It had a positive charge side with three sulfate ion attached, which located in the nucleic acid binding proteins. The protein later was verified as the RNA-binding protein.

Streptococcus pneumonia was commonly discovered in the nasopharynx. It was a bacterium often known as “carriage.” Younger children were prone to the infection. If this organism reached other body parts, it would most likely cause ear infection, sinus infection, and lung infection. If it traveled into the bloodstream it could cause meningitis. This type of disease was known to be invasive, which could lead to dead. This organism was most often found in bacterial meningitis, bacteremia, otitis media and community-acquired pneumonia.


source:
http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?uid=17085




http://www.cdc.gov/ncidod/aip/research/spn.html