A mutant form of polypeptide hormone angiotensin II has the amino acidcomposition(Asp, Arg, Ile, Met, Phe, Pro, Tyr, Val)The following observations are made:Trypsin yields a dipeptide containing Asp and Arg, and a hexapeptidewith all the rest.• Cyanogen bromide cleavage yields a dipeptide containing Phe and Pro,and a hexapeptide containing all the others.• Chymotrypsin cleaves the hormone into two tetrapeptides, ofcomposition(Asp, Arg, Tyr, Val) and (Ile, Met, Phe, Pro)• The dipeptide of composition (Pro, Phe) cannot be cleaved by eitherchymotrypsin or carboxypeptidase.What is the sequence of angiotensin II?

Introduction: The amino acids are combined by an amide or peptide bonds. The series of amino acids…

Answered: A mutant form of polypeptide hormone…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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2. The following tyrosine-phosphorylated polypeptides were tested as substrates of protein tyrosine phosphatase, an important enzyme in cellular signal transduction. The pTyr in bold signifies the tyrosine residue that is phosphorylated. The binding affinities of the polypeptide substrates to the enzyme were found to follow the order: (a) > (c) - (d) >> (b). (a) Asp-Ala-Asp-Glu-pTyr-Leu-lle-Pro-Gln-Gln-Gly (b) Pro-Val-Pro-Glu-pTyr-lle-Asn-Ala-Ser-Val (c) Asp-Ala-Glu-Glu-pTyr-Leu-Val-Pro-Gln-Gln-Gly (d) Asp-Asn-Leu-Tyr-pTyr-Trp-Asp-Glu-Asn-Ser-Ser In addition to the presence of the phosphorylated tyrosine residue, what amino acid a) properties of the polypeptides accounts for the relative order of binding affinities to the enzyme? b) the active site of the phosphatase enzyme that are responsible for the affinity of substrate binding? Assume a pH of 7.4 at the enzyme active site. (Note a phosphatase uses phosphate substrate) What amino acids have side chains that would indicate they are…
E Threonine 6. You have identified some intermediates in threonine synthesis: A, B, C, D and E. You grow a few of your mutants in the presence of these different intermediates to determine the order in which the gene products act. Below are your results. A (+) means growth and a (-) means no growth. Given these data, draw the best possible pathway for the synthesis of threonine. The diagram should use arrows to indicate one intermediate being changed to another intermediate. Indicate which gene produces the product responsible for the conversion by listing the mutant in that gene above the arrow. Mt1 Mt2 Mt4 Mt7
please identify amino acids in the N terminus in the picture below.
. Studies on CAMP actions in cultured cells usually involve adding to the cell culture not CAMP, but dibutyryl CAMP (see structure). Why is this structural modification necessary? How could you test the premise that di-Bu-CAMP has the same biochemical effects as CAMP? N. N= Nat Dibutyryl CAMP O
Compare and contrast the biological roles of the following amino acids the following pairs ofamino acids. Once you have documented these role state which member of the pair is most important and why.
Read very carefully: Chymotrypsin cleaves peptides C TERMINUS to the aromatic amino acids. Trypsin cleaves peptides C TERMINUS to basic amino acids. Cyanogen bromide (CNBR) cleaves C-terminus to methionine residues. With this knowledge, reconstruct the following cleavage products and give the original peptide sequence. CNBR Chymotrypsin WITHHERISALLRIGHT ISTRYWITHM Trypsin EISAM YWITHMEISAMANINGCHEMI STR YWITHHER 1 The which convorted e Name.
1. Glycosphingolipids function via cis regulation and trans recognition. Explain these terms and provide examples of each.
A child with coarse facies, corneal clouding, joint stiffness and mental retardation is found to have a Damage to this enzyme directly affects which of partial defect in N-acetylglucosaminotransferase. the following biochemical functions? A. Formation of polysomes B. Microtubule attachment to centrioles C. Synthesis of ribosomal RNA D. Targeting of enzymes for lysosomes E. Transport of sugars into mitochondria
a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).
Small molecules are used as inhibitors of protein action - as drugs. They most often do this by blocking the active site within the protein. Potential drugs can be screened computationally to determine if they are strongly bound to the protein. Figure 1 shows a possible conformation of a candidate drug molecule, 4-bromo-2- carboxymethylamide-pyrrole (abbreviation: BCMAP) at the active site of a protein (abbreviation: PR). Figure 2 shows the full protein structure whilst figure 3 shows a known inhibitor of the protein at the site, overlayed with another calculated conformer of BCMAP. (a) Explain what types of interactions, both intermolecular and intramolecular, that a molecular mechanics forcefield must be able to describe in order to be able to accurately determine the geometry of BCMAP in the protein. Identify which interactions will be the most important to describe accurately. Figure 1.4-bromo-2-carboxymethylamide-pyrrole (BCMAP) (C, N, O, and Br atoms in yellow, blue, red, and…
What amino acids can be found in chymotrypsin’s specificity pocket? What would happen if one of those amino acids was changed to lysine? In relation to the amino acid in the specificity pocket, which peptide bond is cleaved; C terminal or N terminal? What is this bond’s proximity to the serine in the active site?
Why Phenylmethylsulfonyl fluoride (PMSF, shown in Fig.) does not inhibit aspartate protease as potent as serine protease?

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