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Mutation identity- GLY
Outline the effects the mutation will have on the 3D structure and function of the 3GRS glucathione reducatse protein.
Step by step
Solved in 2 steps
- Mutation identity- GLY Outline the effects the mutation of cysteine with GLY on the 3D structure and function of the 3GRS glucathione reducatse protein.Reposting - What would the tertiary structure of the dipeptide Asp-Ser be if it was made into a polypeptide chain? (Would it form a beta pleated sheet, an alpha helix, etc) Why would it do this? What properties of this polypeptide causes this? This sub part still needs to be solved - What would the tertiary structure of Pro-ala and Glycl-L-alanine be?Molecular detail of spike Y453F
- Leu-Trp-Phe-Met-Ala-Ile-Val- Draw the structure of the peptide at pH7.4. and Indicate the hydrogen bonds formed in the alpha helix.Question:- Based on the figure below, predict what peptide bond could be the substrate of each protease(The bond marked in blue is where hydrolysis occurs, choose 2 peptides per protease type) Chymotrypsin:_________ Trypsin:_________ Elastase:_________ 1. SR−SG 2. SF−SG 3. SK−SG 4. SA−SG 5. SV−SG 6. SM−SGActivity: Write the line structure of each of the following peptide at pH7 and identify how many peptide bond in each number. 1. Glycyl-valyl-serine 2. Threonyl-cysteine 3. Isoleucyl-methionyl-aspartate
- Activity: Write the line structure of each of the following peptide at pH7 and identify how many peptide bond in each number. 1 Alanyl-phenylalanine 2. Lysyl-alanine 3.Phenylalanyl-tyrosyl-leucineEnzyme: Crystal Structure of Wild-Type Human Phosphoglucomutase-1 (PGM1) the description of the mechanism of how this enzyme is regulated (e.g., depending on the enzyme, the mechanism could range from being solely dependent on gene regulation to protein structure-based mechanism).Remember remove the introns! All introns start with GT and end with AG.
- Not the best with titration curves. Identify the position on the following diprotic titration drive where the amino acid has no net charge.The Energetic Cost of Peptide Elongation How many ATP equivalents are consumed for each amino acid added to an elongating polypeptide chain during the process of protein synthesis?Question:- Describe the function of each of the following Shortly. a. Amino-acyl tRNA synthetase b. E coll release factors 1 and 2 (RF1 and RF2) c. 5' methyl-guanosine cap d. Ribosomal P site
