Bundle: Introduction to General, Organic and Biochemistry, 11th + OWLv2, 4 terms (24 months) Printed Access Card
11th Edition
ISBN: 9781305705159
Author: Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres
Publisher: Cengage Learning
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Textbook Question
Chapter 22, Problem 22.71P
22-71 Which amino acid side chain is most frequently involved in denaturation by reduction?
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(11pts total) Consider the arrows pointing at three different carbon-carbon bonds in the
molecule depicted below.
Bond B
Bond A
Bond C
a. (2pts) Which bond between A-C is weakest? Which is strongest? Place answers in
appropriate boxes.
Weakest
Bond
Strongest
Bond
b. (4pts) Consider the relative stability of all cleavage products that form when bonds A,
B, AND C are homolytically cleaved/broken. Hint: cleavage products of bonds A, B,
and C are all carbon radicals.
i. Which ONE cleavage product is the most stable? A condensed or bond line
representation is fine.
ii. Which ONE cleavage product is the least stable? A condensed or bond line
representation is fine.
c. (5pts) Use principles discussed in lecture, supported by relevant structures, to
succinctly explain the why your part b (i) radical is more stable than your part b(ii)
radical. Written explanation can be no more than one-two succinct sentence(s)!
.
3°C
with
TH
12. (10pts total) Provide the major product for each reaction depicted below. If no reaction
occurs write NR. Assume heat dissipation is carefully controlled in the fluorine reaction.
3H
24 total (30)
24
21
2h
• 6H total
● 8H total
34
래
Br2
hv
major product
will be most
Substituted
12
hv
Br
NR
I too weak of a
participate in P-1
F₂
hv
Statistically
most favored
product will be
major
=
most subst =
thermo favored
hydrogen atom abstractor to
LL
F
Five chemistry project topic that does not involve practical
Chapter 22 Solutions
Bundle: Introduction to General, Organic and Biochemistry, 11th + OWLv2, 4 terms (24 months) Printed Access Card
Ch. 22.4 - Problem 22-1 Show how to form the dipeptide...Ch. 22.10 - Problem 22-2 What is the oxidation number (the...Ch. 22.10 - Prob. 22.3PCh. 22.11 - Prob. 22.4PCh. 22 - 22-5 What are the functions of (a) ovalbumin and...Ch. 22 - 22-6 The members of which class of proteins are...Ch. 22 - 22-7 What is the function of an immunoglobulin?Ch. 22 - Prob. 22.8PCh. 22 - 22-9 What is the difference in structure between...Ch. 22 - 22-10 Classify the following amino acids as...
Ch. 22 - 22-11 Which amino acid has the highest percentage...Ch. 22 - Prob. 22.12PCh. 22 - Prob. 22.13PCh. 22 - Prob. 22.14PCh. 22 - Prob. 22.15PCh. 22 - 22-16 Which amino acids in Table 22-1 have more...Ch. 22 - 22-17 What are the similarities and differences in...Ch. 22 - 22-18 Draw the structures of L- and D-valine.Ch. 22 - Prob. 22.19PCh. 22 - 22-20 Show how alanine, in solution at its...Ch. 22 - 22-21 Explain why an amino acid cannot exist in an...Ch. 22 - 22-22 Draw the structure of valine at pH 1 and at...Ch. 22 - Prob. 22.23PCh. 22 - 22-24 Draw the most predominant form of histidine...Ch. 22 - 22-25 Draw the most predominant form of lysine at...Ch. 22 - Prob. 22.26PCh. 22 - 22-27 Show by chemical equations how alanine and...Ch. 22 - 22-28 A tetrapeptide is abbreviated as DPKH. Which...Ch. 22 - 22-29 Draw the structure of a tripeptide made of...Ch. 22 - 22-30 (a) Use the three-letter abbreviations to...Ch. 22 - 22-31 A polypeptide chain is made of alternating...Ch. 22 - Prob. 22.32PCh. 22 - 22-33 Which of the three functional groups on...Ch. 22 - Prob. 22.34PCh. 22 - 22-35 Why is histidine considered a basic amino...Ch. 22 - Prob. 22.36PCh. 22 - Prob. 22.37PCh. 22 - 22-38 Why does proline not absorb light at 280 nm?Ch. 22 - Prob. 22.39PCh. 22 - Prob. 22.40PCh. 22 - Prob. 22.41PCh. 22 - 22-42 (a) How many atoms of the peptide bond lie...Ch. 22 - 22-43 (a) Draw the structural formula of the...Ch. 22 - 22-44 How can a protein act as a buffer?Ch. 22 - 22-45 Proteins are least soluble at their...Ch. 22 - 22-46 How many different tripeptides can be made...Ch. 22 - 22-47 How many different tetrapeptides can be made...Ch. 22 - 22-48 How many amino acid residues in the A chain...Ch. 22 - 22-49 Based on your knowledge of the chemical...Ch. 22 - 22-50 Is a random coil a (a) primary, (b)...Ch. 22 - 22-51 Decide whether the following structures that...Ch. 22 - Prob. 22.52PCh. 22 - 22-53 Do iron and zinc ions play role in protein...Ch. 22 - Prob. 22.54PCh. 22 - 22-55 Consider the coordination compound Fe(CO)5...Ch. 22 - Prob. 22.56PCh. 22 - 22-57 Consider the coordination compound...Ch. 22 - Prob. 22.58PCh. 22 - 22-59 What is the effect of salt bridges on the...Ch. 22 - Prob. 22.60PCh. 22 - 22-61 Polyglutamic acid (a polypeptide chain made...Ch. 22 - 22-62 Distinguish between intermolecular and...Ch. 22 - 22-63 Identify the primary, secondary, and...Ch. 22 - 22-64 If both cysteine residues on the B chain of...Ch. 22 - 22-65 (a) What is the difference in the quaternary...Ch. 22 - Prob. 22.66PCh. 22 - Prob. 22.67PCh. 22 - Prob. 22.68PCh. 22 - Prob. 22.69PCh. 22 - Prob. 22.70PCh. 22 - 22-71 Which amino acid side chain is most...Ch. 22 - 22-72 What does the reducing agent do in...Ch. 22 - 22-73 Silver nitrate is sometimes put into the...Ch. 22 - 22-74 Why do nurses and physicians use 70% alcohol...Ch. 22 - 22-75 (Chemical Connections 22A) Why must some...Ch. 22 - Prob. 22.76PCh. 22 - Prob. 22.77PCh. 22 - Prob. 22.78PCh. 22 - Prob. 22.79PCh. 22 - Prob. 22.80PCh. 22 - Prob. 22.81PCh. 22 - 22-82 (Chemical Connections 22H) How does the...Ch. 22 - Prob. 22.83PCh. 22 - 22-84 How many different dipeptides can be made...Ch. 22 - 22-85 Denaturation is usually associated with...Ch. 22 - Prob. 22.86PCh. 22 - Prob. 22.87PCh. 22 - Prob. 22.88PCh. 22 - 22-89 What kind of noncovalent interaction occurs...Ch. 22 - Prob. 22.90PCh. 22 - 22-91 Which amino acid does not rotate the plane...Ch. 22 - 22-92 Write the expected products of the acid...Ch. 22 - 22-93 What charges are on aspartic acid at pH 2.0?Ch. 22 - Prob. 22.94PCh. 22 - Prob. 22.95PCh. 22 - Prob. 22.96PCh. 22 - 22-97 Gelatin is derived from collagen by...Ch. 22 - Prob. 22.98PCh. 22 - Prob. 22.99PCh. 22 - Prob. 22.100PCh. 22 - 22-101 Using what you know about protein...Ch. 22 - Prob. 22.102PCh. 22 - Prob. 22.103PCh. 22 - 22-104 Why is collagen not a very good source of...Ch. 22 - Prob. 22.105P
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- Please correct answer and don't used hand raitingarrow_forwardQ2. Consider the hydrogenation of ethylene C2H4 + H2 = C2H6 The heats of combustion and molar entropies for the three gases at 298 K are given by: C2H4 C2H6 H2 AH comb/kJ mol¹ -1395 -1550 -243 Sº / J K¹ mol-1 220.7 230.4 131.1 The average heat capacity change, ACP, for the reaction over the temperature range 298-1000 K is 10.9 J K¹ mol¹. Using these data, determine: (a) the standard enthalpy change at 800 K (b) the standard entropy change at 800 K (c) the equilibrium constant at 800 K.arrow_forward13. (11pts total) Consider the arrows pointing at three different carbon-carbon bonds in the molecule depicted below. Bond B Bond A Bond C a. (2pts) Which bond between A-C is weakest? Which is strongest? Place answers in appropriate boxes. Weakest Bond Strongest Bond b. (4pts) Consider the relative stability of all cleavage products that form when bonds A, B, AND C are homolytically cleaved/broken. Hint: cleavage products of bonds A, B, and C are all carbon radicals. i. Which ONE cleavage product is the most stable? A condensed or bond line representation is fine. ii. Which ONE cleavage product is the least stable? A condensed or bond line representation is fine. c. (5pts) Use principles discussed in lecture, supported by relevant structures, to succinctly explain the why your part b (i) radical is more stable than your part b(ii) radical. Written explanation can be no more than one-two succinct sentence(s)! Googlearrow_forward
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