\"I T-Mobile Wi-Fi 8:20 AM blackboard.towson.eduC Take Home Question Given the f
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"I T-Mobile Wi-Fi 8:20 AM blackboard.towson.eduC Take Home Question Given the following diagram of how protein AWESOMEI binds to it's target DNA, describe the potential effects of each of the 5 mutations shown below. The wild-type sequence of helix #1 is also shown in the blue box, and all the mutations are in helix #1 (see numbers for identifying particular residues) helix #1 )-VI-L-Y-F-W-I-M-Y-F-S-H-Y-W-R(16) #1 Predict the consequence of the following mutations 1) Arg(1) to Glu 2) 3) 4) Trp(7) to Ph 5 Met(9) to Pro Arg(1) to Ala Pho(6) to lleExplanation / Answer
Consequences of mutations are as follows:
1. Arginine to glutamate - Arginine is a positively charged amino acid. It is usually found on the surface of proteins. It plays a crucial role in the functionality of the protein. It strongly interacts with the phosphate group of the DNA. Mutation of Arginine to glutamate makes the protein inactive. Thus, the alpha-helix will not interact with the DNA.
2. Arginine to Alanine: Alanine is a non-reactive protien. Hence, mutation of arginine to alanine will again make the protein non-functional. Thus, the alpha-helix will not interact with the DNA.
3. Phenylalanine to isoleucine: Isoleucine is commonly found in the beta-sheets of proteins. Thus, the mutation of phenylalanine to isoleucine may change the conformation of protein from alpha-helix to beta-helix. Due this change, the protein will bind to the major groove of DNA interacting with the DNA bases and in the minor groove it interacts with the sugar and phosphate groups.
4. Tryptophan to Phenylalanine: Tryptophan has shown increased reactivity than phenylalanine. Thus, mutation of tryptophan to phenylalanine reduces the interaction with DNA.
5. Methionine to proline: This mutation introduces kink in the alpha-helix and changes the direction of the alpha-helix.
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