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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Two melanocyte-stimulating hormones have the following amino acid sequences. Take a highlighter or colored pencil, and figure out how much of the sequence the porcine MSH has in common with the human MSH (how much is conserved between the two species). beta-MSH (human): Ala-Glu-Lys-Lys-Asp-Glu-Gly-Pro-Tyr-Arg-Met-Glu-His-Phe-Arg-Trp-Gly-Ser-Pro-Pro-Lys-Asp beta-MSH (porcine): Asp-Glu-Gly-Pro-Tyr-Lys-Met-Glu-His-Phe-Arg-Trp-Gly-Ser-Pro-Pro-Lys-Asp One amino acid interrupts the parts you highlighted in each sequence. Which amino acid was it in each and which category does that amino acid belong to on your amino acid chart? this to make much difference for the cross-species function of beta-MSH (why?)? and Do you expect
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
Draw a structural formula for a nucleoside composed of the following. Q.) a-d-Ribose and adenine
please identify amino acids in the N terminus in the picture below.
Suggest the effects of each of the following mutations on the physiologicalrole of chymotrypsinogen:(a) R15S(b) C1S(c) T147S
Azaserine inhibits amidotransferases. State the purine precursor that resembles azaserine. Which step in the purine biosynthetic pathway will be inhibited?
. 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.
The metabolic amino acid ornithine is a direct precursor of the polyamine putrescine, shown here. + HẠN–CH,CH,CH,CH, NH, + Subsequent reactions convert putrescine to spermine and spermidine. transamination Putrescine What type of reaction is required to convert ornithine to putrescine? O dehydration O methylation O decarboxylation What enzymatic cofactor is needed to convert ornithine to putrescine? O S-adenosylmethionine FeMo O tetrahydrofolate O pyridoxal phosphate

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