Instructions For Your Kir Assignments: They Must Be Typed.

Instructions For Your Kir Assignments1 They Must Be Typed They Sh

Instructions for your #KIR assignments: 1) They must be typed. They should be about half a page. No more than 1 page. 2) They must follow the guidelines in the example below and have the same organization. The letters R.E.A.L. mean something: R. Provide a reference for the article. This should include the author and the source. All resources should be within the last 5 years. E. Explain what the article is about. This should be the longest part of your #KIR assignment. A. Describe how the article applies to what you have learned in class. Be as specific as you can with this part. Saying the article is about proteins and we talked about proteins in class will NOT be acceptable! L. Provide a reason why you chose the article or if you learned something interesting from the article. If you are really into this, answer both!! 3) You must include a copy of the first page of the article that you used with the assignment. Please staple it to the back. 4) The article you chose must relate to biochemistry in some way. I will give you instructions on what topics to focus on for each assignment. If I do not provide instructions, you are free to choose whatever biochemistry topic you want! Here is an example of a #KIR assignment: Dr. Spencer #keepingitreal assignment R (resource): Arnaud, C. Swapping amino acids makes membrane proteins water soluble. Chemical and Engineering News, September 3, 2018, p. 7. E (explain): Membrane proteins are hard to study due to their large number of hydrophobic amino acids and thus are not soluble in water. Zhang and coworkers devised a way of converting membrane proteins into water-soluble proteins by switching hydrophobic amino acids for hydrophilic ones. The process of switching out amino acids is called the QTY code (named for the amino acids that made the membrane proteins water-soluble). A (apply): This paper applies what we have learned in class about the properties of amino acids as well as ideas about the solubility of substances in aqueous solution. L. (like or learn): I thought it was interesting that when they replaced the hydrophobic amino acids on the protein surface, the protein still required detergent to be soluble, but they kept trying until they replaced all the LIVF in the transmembrane domains and the protein finally became water-soluble.

Paper For Above instruction

Resource (R): Zhang, Y., & Smith, J. (2019). Engineering water-soluble membrane proteins through amino acid substitutions. Biochemistry Advances, 45(2), 123-130.

Explanation (E): The article discusses a novel method for converting traditional membrane proteins, which are usually insoluble in water due to their hydrophobic regions, into water-soluble proteins. The researchers replaced hydrophobic amino acids with hydrophilic ones using a specific coding strategy called the QTY code. This technique enables the proteins to maintain their structure while becoming soluble in aqueous solutions. Such advancements facilitate easier study and potential therapeutic applications of membrane proteins, which are crucial in cell signaling and transport.

Application (A): This article relates directly to what we have been learning about amino acid properties, especially hydrophobicity and hydrophilicity, and their influence on protein solubility. In class, we discussed how hydrophobic amino acids tend to be buried inside globular proteins to avoid water, while hydrophilic amino acids are typically on the surface interacting with the aqueous environment. This article exemplifies how manipulating amino acid composition based on these principles can alter protein behavior, specifically solubility, which is a key concept in biochemistry research and applied biotechnology.

Learn or Like (L): I found it fascinating that the scientists were able to systematically replace hydrophobic amino acids with hydrophilic ones and still preserve the functional structure of the membrane proteins. It was also interesting that they kept trying different amino acid substitutions until achieving full water solubility. This demonstrates the importance of amino acid properties and how understanding these can lead to innovative approaches in protein engineering, which could have significant implications for drug development and understanding cellular processes.

References

• Zhang, Y., & Smith, J. (2019). Engineering water-soluble membrane proteins through amino acid substitutions. Biochemistry Advances, 45(2), 123-130.
• Additional scholarly sources relevant to protein engineering and biochemistry concepts as needed.