The 20 different amino acids found in polypeptides exhibit different chemical and physical properties because o- different.. a. Amino groups attached to an alpha carbon O b. Side chains (R groups) Oc. Asymmetric carbons O d. Carboxyl groups attached to an alpha carbon O e. Alpha carbons
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- Text:QUESTION 16 Protein maturation in the ER includes. A Disulfide bond formation B. proteolytic cleavage C attachment of oligosaccharide d. Prolyl isomertzationPlease ASAP. Thank you. How does the mutation change/affect the structure of the Hb heterotetramer (ie how is quaternary protein structure affected)?Question 9. Which of thefollowing is not formed through adehydration synthesis reaction?A. polysaccharideB. polypeptideC. Nucleic acidD. phospholipidE. glycerol
- I was given an amino acid position 564 with the PDC code 2V1X. Would it be possible to describe why this position in the protein is important and outline the effects the mutation will have on the structure / function of the protein? Thank you.Q04:- Linear sequence of amino acids within a protein is known as-- a. primary structure b. secondary structure c. tertiary structure d. quaternary structureQUESTION 6 What is the three ketter code for each peptide(a) KFYV(b) ERSC(c) PIMFThe 3-letter code for Peptide (a) is: The 3-letter code for Peptide (b) is: The 3-letter code for Peptide (c) is:
- Good day can you please help me with the question below. Your assistance will be highly appreciated. Explain how the spectroscopic properties of amino acids can be used to quantify protein using UV light.Solve only the specific amino acid number and percent (%) Difference. Thank you so much♥Time remaining: 00:08:55 Chemistry Consider a peptide with the following amino acid sequence: H2N-ASENHLDGCPYTKSRG-COOH Analyze the predominate protonation state and thus dominate charge (+1, 0, -1) of the residues in this peptide at pH 3, 6, and 10 by filling in the table below, identifying the relevant pKa appropriate for each residue. (Note that choice of pKa and its. application will be graded independently; e.g., if you can choose the wrong pKa but apply it correctly, you will lose points only for the pKa.) AA Residue pKa Charge pH 3 Charge pH 6 Charge pH 10 A S E N H L D G C P Y T K S R G
- Question 10 (2 points) A protein heterodimer would be considered an example of: -primary structure -secondary structure -tertiary structure -quaternary structure -atomic structureWhich statement is true regarding denaturation process? Question 21 options: Protein experiences hydrolysis as it denatures and alters its structure. Denaturation is the process of altering the shape of a protein that involves breaking the amide bonds. Denaturation is the process of altering the shape of a protein without breaking the amide bonds. As protein denatures, new peptide bonds form with the added amino acids.Unsaturated fatty acids have ----. Question 16 options: multiple amide groups in their hydrocarbon chain. one or more double bonds in their long hydrocarbon chain. one or more single bonds in their long hydrocarbon chain. multiple aldehyde groups in their long hydrocarbon chain.