Biochemistry: Concepts and Connections (2nd Edition)
2nd Edition
ISBN: 9780134641621
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Chapter 8, Problem 11P
The following data describe the catalysis of cleavage of peptide bonds small peptides by the enzyme elastase.
The arrow indicates the peptide bond cleaved each case.
a. If a mixture of these three substrates was presented to elastase with the concentration of each peptide equal to 0.5 mM, which would be digested most rapidly? Which most slowly? (Assume enzyme present in excess.)
b. On basis of these data, suggest what features of amino acid sequence dictate the specificity of proteolytic cleavage by elastase.
c. Elastase is closely related to chymotrypsin. Suggest two kinds of amino acid residues you might expect to find in or near the active site.
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The following data describe the catalysis of cleavage of peptide bonds in small peptides by the enzyme
UTSASE (the arrow indicates the peptide bond cleaved in each case).
Substrate
Km(mM)
kcat(s)
PAPALG
4.0
26
РАPАLA
1.5
37
РАРАLF
0.64
18
Based on the above data shown for UTSAse what features of amino acid sequence dictate the specificity of
the proteolytic cleavage?
A. Large hydrophilic R-groups
B. Large hydrophobic R-groups
C. Neutral R-groups
D. Small hydrophilic R-groups
E. Large hydrophobic R-groups
F. Negatively charged R-groups
G. Positively charged R-groups
The following data describe the catalysis of cleavage of peptide bonds insmall peptides by the enzyme elastase. The arrow indicates the peptide bond cleaved in each case.(a) If a mixture of these three substrates was presented to elastase withthe concentration of each peptide equal to 0.5 mM, which would bedigested most rapidly? Which most slowly? (Assume enzyme is presentin excess.)(b) On the basis of these data, suggest what features of amino acid sequence dictate the specificity of proteolytic cleavage by elastase.(c) Elastase is closely related to chymotrypsin. Suggest two kinds of aminoacid residues you might expect to find in or near the active site.
The ESI-MS spectrum in positive ionization mode for lysozyme is obtained.
a. What is the molecular weight of the protein to 5 significant figures based on the two highlighted ion species?
b. What is the charge of the peaks at 1101.5 and 1789.2.
Chapter 8 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
Ch. 8 - Prob. 1PCh. 8 - The enzyme urease catalyzes the hydrolysis of urea...Ch. 8 - An enzyme contains an active site aspartic acid...Ch. 8 - The folding and unfolding rate constants for a...Ch. 8 - In some reactions, in which a protein molecule is...Ch. 8 - Would you expect an “enzyme” designed to bind to...Ch. 8 - The initial rate for an enzyme-catalyzed reaction...Ch. 8 - a. If the total enzyme concentration in Problem 7...Ch. 8 - Prob. 9PCh. 8 - Prob. 10P
Ch. 8 - The following data describe the catalysis of...Ch. 8 - At 37 oC, the serine protease subtilisin has kcat...Ch. 8 - The accompanying figure shows three...Ch. 8 - The steady-state kinetics of an enzyme are studied...Ch. 8 - The same enzyme as in Problem 14 is studied in the...Ch. 8 - Enalapril is an anti-hypertension “pro-drug"...Ch. 8 - Initial rate data for an enzyme that obeys...Ch. 8 - Prob. 18PCh. 8 - Suggest the effects of each of the following...Ch. 8 - The inhibitory effect of an uncompetitive...Ch. 8 - Prob. 21PCh. 8 - Prob. 22PCh. 8 - Prob. 23PCh. 8 - In kinetics experiments, the hydrolysis of the...
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- Partial hydrolysis of a protein yielded a number of polypeptides. One of them was purified. Deduce the sequence of amino acids in this polypeptide from the following information: (a) Complete acid hydrolysis yielded ala + arg + 2ser + lys + phe + met + trp + pro (b) Treatment with fluorodinitrobenzene (FDNB, the Sanger reagent) followed by complete acid hydrolysis yielded dinitrophenylalanine (DNP-ala) and a dinitrophenyllysine (e-DNP-lys) as the only DNP derivatives. (c) Neither carboxypeptidase A nor carboxypeptidase B released a C-terminal amino acid. (d) Treatment with cyanogen bromide (CNBr) yielded two peptides: One contained ser + trp + pro. The other contained all the remaining amino acids (including the second ser). (e) Treatment with chymotrypsin yielded three peptides. One contained only ser + pro. Another contained only met + trp. The third contained phe + lys + ser + arg + ala. (f) Treatment with trypsin yielded three peptides. One contained only ala + arg. Another…arrow_forwardBovine pancreatic trypsin inhibitor (BPTI; as shown) contains six cysteine residues that form three disulfide bonds in the native structure of BPTI. Suppose BPTI is reduced and unfolded in urea (as illustrated for RNase A as shown). If the reduced unfolded protein were oxidized prior to the removal of the urea, what fraction of the resulting mixture would you expect to possess native disulfide bonds?arrow_forwardSuppose that there is a protein consisting of two polypeptide chains with the given sequences in the picture. Answer the following questions. a. What digestion or cleavage agent(s) should a biochemist use to determine the sequence of subunit α? Explain why. b. What digestion or cleavage agent(s) should a biochemist use to determine the sequence of subunit β? Explain why. c. Identify the resulting peptide fragment(s) of subunit α. Identify the resulting peptide fragment(s) of subunit β.arrow_forward
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