A NONAPEPTIDE that attacks and kills cancer cells has just been recently isolated from a rare fungus. Amino acid analysis of the peptide reveals the followinginformation below: (NOTE: when the sequence is not known, a comma separates the amino acids)HytrezineAcid tydrolysis (6 N HC) at 110CNonapeptide(2) Arg. Gin, (2) Tyr, Gly, Ser, Thr, and Met24-dinitrofieorebenzeneDNP-ThrGin andmodified freePeptide 1(Arg. Thr, Ser)amino acidsCleavoge with Trypsin, then chrametogruphyPeptide 2(Gly. Tyr, Arg)MetTripeptide(yanopen bromideDipeptideCleovege with Chymetrypsin, then chromatograophyPeptide 3(Arg, Ser, Tyr, Thr)Amino acidPeptide 4(Gly, Arg. Tyr) When answering the questions below, please use the one-letter code for the amino acid, with NO spaces and symbols between each letter.1. What is the N-terminal AA residue?2. What is the C-terminal AA residue?3. What is the sequence of Peptide 1?4. What is the sequence of Peptide 4?5. What is the overall amino acid sequence?

Aminoacids are organic compunds. that combine to form protein. Amino acid is formed when a central…

Answered: 1. What is the N-terminal AA residue?…

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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3. Which best describes the contribution of tertiary (3’) structure of to the native conformation of polypeptides and proteins: a) Structure that results from intrachain interactions of amino acid side chains b) Structure that results from interchain interactions of amino acid side chains c) Structure that results from base pairing d) Structure that results from the linear sequence of amino acids from beginning to end of molecule
1. Sickle cell anemia results from a substitution of a valine for a glutamic acid. What do you expect the effect might be if the mutation were to have placed a leucine at that site? An aspartic acid? 2. Of the following amino acids, glycine, isoleucine, and lysine, which would you expect to be the most soluble in an acidic aqueous solution? Which the least? 3. How many structural isomers could be formed from a molecule with the formula C5H12? C4H8?
1. Amino Acid 1 = W + X = 1 Draw amino acid 1 at a low pH a) As the D Fisher Projection Name of amino acid 1: b) As the S isomer: Arginine
What is the difference between a peptide and a protein? 2. What type of bond is the peptide bond? Explain why the peptide bond is rigid. 3. The pentapeptide Gln-Tyr-Asn-Ala-Asp is present in human cerebrospinal fluid, and its concentration increases in demyelinating diseases. In these diseases, the myelin sheath of nerves is damaged and impairs the conduction of nerve signals. a. What is the N-terminal amino acid? b. What is the C-terminal amino acid? c. How many peptide bonds does this pentapeptide contain? From how many amino acids is this pentapeptide derived? d. Write the structure, the three-letter designation and the IUPAC name of this pentapeptide.
6) Proline is not commonly found in the middle of a-helices because its ring structure prevents it from adopting the proper value and because it disrupts the hydrogen-bonding pattern of the helix. Looking at the structure of proline in the amino acid sequence below, suggest how this residue would disrupt the hydrogen-bonding pattern of an a-helix. 'N H R N N H *** R
How can the 4 nucleotides present in DNA code for the 20 different amino acids found in proteins? How many bases would be needed in a codon if there were five RNA bases instead of four?
4. Which best describes the contribution of quaternary (4’) structure of polypeptides to the native conformation of proteins: a) Structure that results from intrachain interactions of amino B) Structure that results from interchain interactions of amino acid side chains c) Structure that results from base pairing d) Structure that results from the linear sequence acid side chains of amino acids from beginning to end of molecule
1. You are working in a bioengineering lab, and you are asked to create a peptide with a helix with length of 3 nm, a beta strand with length of 35 Å, and a linker containing 25 amino acid residues. a. How many amino acid residues are in this peptide? b. What is the mass of the peptide? 2. Why is quinary structure necessary for a full understanding of how drugs work in cells?
9. Identify the N-terminal and C-terminal amino acid in each peptide. H,N-CH-C-Ņ–CH-C-o- CH2 H CH3 ČH(CH3)2 HÑ-CH-C-Ņ-CH-C-N–CH–C-O- CH2 H ČH3 H ČH,CH,CONH, a.
8.ldentify each of the amino acid in the polypeptide and then name it using the 3-letter abbreviations. H2N- CH- CH- CH CH- CH- OH CH2 CH2 CH-OH CH2 CH2 CH2 Cн CH2 CH2 NH NH ENH NH2
6) Circle one amino acid in this peptide (hint: draw lines between not through atoms). Kahalalide F NH HN HO NH HN HN
2. Of the two sequences, which is more likely to have helical structure. Explain. a) -Glu-Asp-Glu-Glu-Asp-Leu- b) -Glu-Leu-Asp-Arg-Val-Lys-

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1. What is the N-terminal AA residue? 2. What is the C-terminal AA residue? 3. What is the sequence of Peptide 1? 4. What is the sequence of Peptide 4? 5. What is the overall amino acid sequence?