Case B: An oligopeptide has the ff amino acid composition: 2 Phe, 2 Met, 2 Glu, 1 Arg, 1 Val, 1 Leu, 1 Lys, 1 Gly, 1 SerThe reaction of the intact peptide with Sanger reagent followed by acid hydrolysis creates a derivative of Met.Specific cleavage of the intact peptide (using chymotrypsin) produces fragments with the ff sequences:Fragment A: Glu-Gly-Lys-PheFragment B: Met-Ser-Leu-ArgFragment C: Met-Val-Glu-PheQuestion: What information do these result give about the sequence of the peptide?

Peptides are formed of amino acids connected through an amide/peptide bond. The peptide bond is…

Answered: Case B: An oligopeptide has the ff…

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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A polypeptide is digested with trypsin, and the resulting segments are sequenced: Val-Gly Ala-Ala-Gly-Leu-Trp-Arg Arg-Asp-Pro-Gly-Lue-Met-Val-Leu-Tyr-Ala-Ala-Asp-Glu-Lys And the following fragments are produced by chymotrypsin fragmentation: Ala-Ala-Gly-Leu-Trp Arg-Arg-Asp-Pro-Gly-Leu- Met-Val-Leu-Tyr Ala-Ala-Asp-Glu-Lys-Val-Gly What is the sequence of the whole original polypeptide? (Recall that trypsin cleaves a polypeptide backbone at the C-terminal side of Arg or Lys residues, whereas chymotrypsin cleaves after aromatic amino acid residues).
Changing one amino acid within a protein sequence from a tryptophan to a stop codon would be best classified as Amino acids groups Group Characteristics Names Ala, Val, Leu, Ile, Pro, Phe Trp, Met Ala: A Leu: L non-polar hydrophobic Arg: R Asn: N Lys: K Met: M Asp: D Cys: C Gly: G polar hydrophilic (non-charged) Gly , Ser, Thr, Cys, Tyr, Asn Gln Phe: F Pro: P Ser: S acidic negatively charged Asp, Glu Glu: E Gln: Q Thr: T His: H lle: I Trp: W Туr: Y Val: V basic positively charged Lys, Arg, His A) Conservative missense O B) Nonsense O C) Neutral O D) Non-conservative missense
4
Can the same pepptide be used in multiple different proteins? yes or no, explain.
Use the one letter code to give the sequence of this peptide
PEPTIDE #1: Pro-Phe-Thr-Cys PEPTIDE #2: Gly-Tyr-Ser-Asp Calculate the pI of both peptides. Which is more acidic and why? Which one is more hydrophobic? Which peptide sequence (#1 or #2) would be more likely situated on the surface of the protein?
A decapeptide was analyzed and the following information obtained. Determine the primary structure of the peptide. Edman's Degradation: PTH-Ala Trypsin produces 3 peptides of the following composition: 1. Gly, His 2. Ala, Leu, Lys, Val 3. Arg (2), Phe, Pro Chymotrypsin produces 2 peptides of the following composition: 1. Ala, Leu, Lys, Phe, Val 2. Arg (2), Gly, His, Pro Elastase produces 1 amino acids and 3 peptides 1. Ala 2. Leu, Val 3. Arg (2), Lys, Phe, Pro, Gly, His Arg Gly His Leu Phe Pro Val
An oligopeptide has the following amino acid sequence: NH2-Ala-Glu–Leu–Trp–Tyr-Ser–Gly–Lys–Leu-Ala–Arg-Ala-Phe-Ile-Pro–Gly-COOH a) Estimate the net electric charge of the molecule at pH 8.0 and pH 11.0. b) If the above peptide is passed through a cation exchange chromatographic column (that is, the matrix of the column has negative charges) stabilized at pH 8.0, would you expect it to be retained on the column? c) Indicates the number of fragments, and the sequence of each of them, that would be obtained when treating the peptide in question with: i) trypsin, ii) chymotrypsin.
The sequence of crinia-angiotensin, an angiotensin II-like undecapeptide from the skin of the Australian frog, is determined. A single round of Edman degradation releases DNP-Ala. A second round sample of the peptide is then treated with chymotrypsin. Two fragments are released with the following amino acid composition: fragment 1: (H,P,F,V) and fragment 2 (A,D,R,G,P,I,Y). Next, a third sample of the peptide was treated with trypsin, which results in two fragments with the following amino acid compositions: fragment III (A,D,R,G,P) and fragment IV ( H,I,P,F,Y,V). Treatment of another sample with elastase yields three fragments, two of which are sequenced: fragment V (H-P-F) and fragment VI (A-P-G). What is the sequence of the undecapeptide?
A protein has been sequenced after cleavage of disulfide bonds. The protein is known to contain 3 Cys residues, located as shown here. Only one of the Cys has a free —SH group, and the other two are involved in an —S—S— bond. The only methionine and the only aromatic amino acid (Phe) in this protein are in the positions indicated. Cleavage of the intact protein (i.e., withdisulfide bonds intact) by either cyanogen bromide or chymotrypsin does not break the protein into two peptides. Where is the —S—S— bond (i.e., AB, BC, or AC)?
Identify the nitrogen-containing base, sugar and nucleotide name for each of the following item. AMP Name nitrogen-containing base sugar nucleotide dTMP
A At pH 5, what is the net charge of the peptide Val-His-Gln-Cys-Ser-Lys? 0 -1 0 0+1 Ⓒ +2 Q Search "de 96 5 ******* ******* 131183 J- C 8 a hp

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