BIOCHEMISTRY-ACHIEVE (1 TERM)
9th Edition
ISBN: 9781319402853
Author: BERG
Publisher: MAC HIGHER
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Chapter 3, Problem 27P
Interpretation Introduction
Interpretation:
The sequence of the peptide consisting of 14 amino acids should be determined.
Concept introduction:
Trypsin cleaves peptide chains at the carboxyl side of the amino acids lysine (K) or arginine (R) if they are not followed by proline. Carboxypeptidase hydrolyzes the first peptide bond at the C-terminal of the peptide chain except for arginine (R), lysine (K) or proline (P). Chymotrypsin cleaves the peptide bond at the C-terminal where there ishydrophobic amino acids like tyrosine (Y), tryptophan (W), phenylalanine (F), leucine (L) and methionine (M). Cyanogen bromide hydrolyzes peptide bond at C-terminal of methionine residues. Homoserine is a product of cyanogen bromide cleavage by degradation of methionine.
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A protein was completely digested with trypsin and an internal peptide (i.e. not derived
from the N- or C-terminals) was purified. Determine its sequence from the following information:
a) amino acid analysis yields one mole of D, T, P, L, Y, F, K, and R per mole of peptide;
b) treatment of the intact peptide with FDNB, followed by acid hydrolysis, gives DNP-L and &-DNP-K;
c) treatment of the intact peptide with chymotrypsin yields a tripeptide containing K, T, and D; a
tetrapeptide containing P, L, F, and R, and free tyrosine;
d) the tripeptide, in part c, yields DNP-T and ɛ-DNP-K after reaction with FDNB and acid hydrolysis.
Note: trypsin will not cleave on the carboxyl side of arginine or lysine if the next amino acid (donating the
amino group) is proline.
Put your answer here:
pls answer the following question.
-Which amino acids contain the following?a.sulfur/sulfhydryl group
b. aromatic group
c. imidazole ring
d. guanidine group
e. indole group
-Classify the following proteins according to their biological function: casein, albumin gluten, and myoglobin.
-Which levels of protein structure organization are lost during hydrolysis and denaturation?
-What is the Beer-Lambert's Law? Why is it relevant to the quantitative analysis of proteins?
-What are the other protein components of milk aside from casein?
(a) How is ubiquitination attached to the protein of interest? At which amino acid residue(s)? What enzyme(s) is involved, if any?(b) Is the ubiquitination relatively stable or highly dynamic? how does ubiquitination become detached from the protein of interest? what enzyme is involved?(c) what is the function of ubiquitination
Chapter 3 Solutions
BIOCHEMISTRY-ACHIEVE (1 TERM)
Ch. 3 - Prob. 1PCh. 3 - Prob. 2PCh. 3 - Prob. 3PCh. 3 - Prob. 4PCh. 3 - Prob. 5PCh. 3 - Prob. 6PCh. 3 - Prob. 7PCh. 3 - Prob. 8PCh. 3 - Prob. 9PCh. 3 - Prob. 10P
Ch. 3 - Prob. 11PCh. 3 - Prob. 12PCh. 3 - Prob. 13PCh. 3 - Prob. 14PCh. 3 - Prob. 15PCh. 3 - Prob. 16PCh. 3 - Prob. 17PCh. 3 - Prob. 18PCh. 3 - Prob. 19PCh. 3 - Prob. 20PCh. 3 - Prob. 21PCh. 3 - Prob. 22PCh. 3 - Prob. 23PCh. 3 - Prob. 24PCh. 3 - Prob. 25PCh. 3 - Prob. 26PCh. 3 - Prob. 27PCh. 3 - Prob. 28PCh. 3 - Prob. 29PCh. 3 - Prob. 30PCh. 3 - Prob. 31P
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- Determine the sequence of the following 10-mer of ferritin using the data below. i. Complete acid hydrolysis of the 10-mer results in identification of 1A, 1D, 1E, 1F, 1H, 1K, 2L, 1T, 1Y ii. Digestion of the 10-mer with chymotrypsin results in 3 fragments containing (D, H, K, T), (F, L) and (A, E, L, Y) iii. Digestion of the 10-mer with V8 protease, which cuts on the C-side of acidic amino acids, results in three fragments containing (D, F, L, Y), (A, E, L) and (H, K, T) iv. Digestion with trypsin results in a fragment H-T and a fragment with all the other amino acids v. Treatment of the 10-mer with FDNB followed by complete acid hydrolysis results in the following two derivatives, DNP-1 and DNP-2 vi. Treatment of the 10-mer with a carboxypeptidase results in a free threoninearrow_forward11. Below is a folding energy funnel describing folding energy landscape of a protein. The width of the funnel indicates the entropy of the protein, and the height corresponds to the free energy. A) If A is the native fold structure, which state is a molten globule? How does this state differ from A in term of structures. B) Does this protein have multiple folding pathways or just one? C) which state has the lowest free energy? D) According to the width of the funnel, the native state B of the protein has the lowest entropy. If the protein fold A spontaneously to this state, does it violate the 2nd law of thermodynamics? Why or why not? (Hint: in the folding funnel, only the entropy of the protein alone is considered). E) Does the native state also have the lowest enthalpy. What makes the enthalpy decrease as the protein folds? 12. List four methods by which a protein can be denatured and briefly describe how these methods act to disrupt protein structure.arrow_forwardPurification of a protein of unknown structure has been achieved. The natural protein has a molecular weight of 240,000, according to size-exclusion chromatography. Using a concentration of 6 M guanidine hydrochloride in the chromatography, a single peak can be identified as the molecular weight (MW) 60,000 of a protein. B-mercaptoethanol (BME) and guanidine hydrochloride (GHC) are used in tandem to produce proteins with mass masses of 34,000 and 26,000, respectively. The structure of this protein can be inferred from these facts.arrow_forward
- A/B: 3. Amino acid residues and peptide bonds (a) Draw the chemical structure of F, S and H joined by peptide bonds and also connected to neighboring residues as found in a protein. (b) Include all charges as expected at physiological pH (pH = 7.5) () Rank these three amino acid residues by hydrophobicity, pKa, and by nucleophilicity (d) For the central amino acid residue, identify the phi and psi dihedral angles by drawing a curved arrow indicating rotation about the chemical bond. (e) What group(s) eclipse each other if Phi = 0 degrees? Words and Pictures. (f) While Phi = 0 is not well tolerated, Psi = 0 is not uncommon, a so-called “allowed" but not most-favored region of the Ramachandran plot. What group(s) eclipse each other if Psi = 0 degrees and why is this less problematic than the situation created by Phi = 0. Words and Pictures H₂N* Pka: 9.13 H₂C с C._hydrophobicity: 1. phenylalanine (most) 2. Serine 3. Histidinelleast) ده H H. HIN OH I CH₂ CHO pka: 1. Serine (nighest) 2.…arrow_forwarda. An oligopeptide ALVGALGATPTPQMWSHSWRGVSIKS was digested with trypsin.Which method would be most appropriate for separating the products: ion exchange or gel filtration chromatography? Explain.b. Suppose that the peptide was digested with cyanogen bromide. What would be the optimal separation technique? Explainarrow_forwardDetermine the sequence of the decapeptide given the following information below. The decapeptide was hydrolyzed and confirmed to contain these amino acids: E, F, K, M, Q, S, T x 3, W Edman degradation product of the decapeptide: T trypsin fragments: a tetrapeptide (F,K,Q,T) and a hexapeptide (E,M,S,2T,W) chymotrypsin fragments: free S, a dipeptide (F,T) and a heptapeptide (E,K,M,Q,T,T,W) CNBr treatment of the heptapeptide (E,K,M,Q,T,T,W) yielded a tetrapeptide (K,T,M,Q) and a tripeptide (E,T,W) Edman degradation product of (E,T,W): E Use one-letter abbreviations only. One amino acid per blank.arrow_forward
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