EBK BIOCHEMISTRY
6th Edition
ISBN: 8220102959286
Author: GRISHAM
Publisher: CENGAGE L
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Chapter 5, Problem 3P
Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book.
Solving the Sequence of an Oligopeptide From Sequence Analysis Data Amino acid analysis of a decapeptide revealed the presence of the following products:
The following facts were observed:
- Neither car boxy peptidase A nor B treatment of the- decapeptide had any effect.
- Trypsin treatment yielded two tetrapcptides and free Lys.
- Clostripain treatment yielded a tetrapcptide and a hexapeptidc.
- Cyanogen bromide treatment yielded an octapeptide and a dipeptide of sequence NP (using the one-letter codes).
- Chymotrypsin treatment yielded two tripeptides and a telrapeptide. The N-terminal chymotryptic peptide had a net charge of — 1 at neutral pi I and a net charge of —3 al pH 12.
- One cycle of Ed man degradation gave the PTH derivative
What is the ammo acid sequence of this decapeptide?
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Fura-2 Fluorescence (Arbitrary Unit)
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[Ca2+]=2970nM, 25°C
[Ca2+] 2970nM, 4°C
[Ca2+]=0.9nM, 25°C
[Ca2+] = 0.9nM, 4°C
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Wavelength (nm)
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The figure on the LHS shows the excitation spectra of Fura-2 (Em
= 510 nm) in 2 solutions with two different Ca2+ ion concentration
as indicated. Except for temperature, the setting for excitation &
signal acquisition was identical.<
ப
a) The unit in Y-axis is arbitrary (unspecified). Why? <
<
b) Compare & contrast the excitation wavelength of the Isosbestic
Point of Fura-2 at 25 °C & 4 °C. Give a possible reason for the
discrepancy. <
c) The fluorescence intensity at 25 °C & 4 °C are different. Explain
why with the concept of electronic configuration. <
Chapter 5 Solutions
EBK BIOCHEMISTRY
Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...
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- Draw out the following peptide H-R-K-E-D at physiological pH (~7.4). Make sure toreference table 3.1 for pKa values.arrow_forwardThe table provides the standard reduction potential, E', for relevant half-cell reactions. Half-reaction E'° (V) Oxaloacetate² + 2H+ + 2e malate²- -0.166 Pyruvate + 2H+ + 2e → lactate -0.185 Acetaldehyde + 2H+ + 2e¯ →→→ ethanol -0.197 NAD+ + H+ + 2e--> NADH -0.320 NADP+ + H+ + 2e →→ NADPH Acetoacetate + 2H+ + 2e¯ - -0.324 B-hydroxybutyrate -0.346 Which of the reactions listed would proceed in the direction shown, under standard conditions, in the presence of the appropriate enzymes? Malate + NAD+ oxaloacetate + NADH + H+ Malate + pyruvate oxaloacetate + lactate Pyruvate + NADH + H+ lactate + NAD+ Pyruvate + p-hydroxybutyrate lactate + acetoacetate Acetaldehyde + succinate ethanol + fumerate Acetoacetate + NADH + H+ → B-hydroxybutyrate + NAD+arrow_forwardArrange the four structures in order from most reduced to most oxidized. Most reduced R-CH2-CH3 R-CH2-CH₂-OH R-CH,-CHO R-CH₂-COO Most oxidizedarrow_forward
- for each pair of biomolecules, identify the type of reaction (oxidation-reduction, hydrolysis, isomerization, group transfer, or nternal rearrangement) required to convert the first molecule to the second. In each case, indicate the general type of enzyme and cofactor(s) c reactants required, and any other products that would result. R-CH-CH-CH-C-S-COA A(n) A(n) A(n) A(n) Palmitoyl-CoA R-CH-CH=CH-C-S-CoA ° trans-A-Enoyl-CoA reaction converts palmitoyl-CoA to trans-A2-enoyl-CoA. This reaction requires and also produces Coo HN-C-H CH₂ CH₂ CH CH CH, CH, L-Leucine CH, CH, D-Leucine 8/6881 COO HÌNH: reaction converts L-leucine to D-leucine. This reaction is catalyzed by a(n) H-C-OH H-C-OH C=0 HO-C-H HO-C-H H-C-OH H-C-OH H-C-OH CH,OH Glucose H-C-OH CH,OH Fructose OH OH OH CH-C-CH₂ reaction converts glucose to fructose. This reaction is catalyzed by a(n) OH OH OPO I CH-C-CH H Glycerol Glycerol 3-phosphate H reaction converts glycerol to glycerol 3-phosphate. This reaction requires H,N- H,N H…arrow_forwardAfter adding a small amount of ATP labeled with radioactive phosphorus in the terminal position, [7-32P]ATP, to a yeast extract, a researcher finds about half of the 32P activity in P; within a few minutes, but the concentration of ATP remains unchanged. She then carries out the same experiment using ATP labeled with 32P in the central position, [ẞ-³2P]ATP, but the 32P does not appear in P; within such a short time. Which statements explain these results? Yeast cells reincorporate P; released from [ß-³2P]ATP into ATP more quickly than P¡ released from [y-³2P]ATP. Only the terminal (y) phosphorous atom acts as an electrophilic target for nucleophilic attack. The terminal (y) phosphoryl group undergoes a more rapid turnover than the central (B) phosphate group. Yeast cells maintain ATP levels by regulating the synthesis and breakdown of ATP. Correct Answerarrow_forwardCompare the structure of the nucleoside triphosphate CTP with the structure of ATP. NH₂ 0- 0- 0- ·P—O—P—O—P—O—CH₂ H H H H OH OH Cytidine triphosphate (CTP) Consider the reaction: ATP + CDP ADP + CTP NH 0- 0- 0- ¯0— P—O— P—O—P-O-CH₂ H Η о H H OH OH Adenosine triphosphate (ATP) NH₂ Now predict the approximate K'eq for this reaction. Now predict the approximate AG for this reaction. Narrow_forward
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