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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Textbook Question
Chapter 2, Problem 21P
Is RNA-binding enzyme RNase A more likely to have a pl of 9.2 or 5.0? Briefly explain your reasoning.
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Is RNA-binding enzyme RNase A more likely to have a pI of 9.2 or 5.0?Briefly explain your reasoning.
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Name
Class
Date
Interpreting Diagrams: Understanding the Main Ideas
The Genetic Code (MRNA)
Lysine
Lysine
Asparagine
Asparagine
Arginine
Arginine
Serine
Serine
Isoleucine
Methionine
Isoleucine
Isoleucine
Threonine
Threonine
Threonine U
Threonine c
Glutamic acid Glycine
Glutamic acid Glycine
Aspartic acid Giycine
Aspartic acid Glycine
Valine
Valine
Valine
Valine
Alanine
Alanine
Alanine
Alanine
"Stop" codon "Stop" codon Leucine
Trytophan
Cysteine
Cysteine
Al
Gl
"Stop" codon
Tyrosine
Тугosine
Serine
Serine
Phenylalanine Serine
Phenylalanine Serine
Leucine
Glutamine
Giutamine
CHistidine
Histidine
Arginine
Arginine
Arginine
Arginine
Al
Leucine
Leucine
Leucine
Loucine
Proline
Proline
Proline
Proline
Icl
A
G
Second Base in Code Word
Use the information in the accompanying figure to complete the following
table. The first row has been completed to help you get started.
DNA codon
MRNA codon
IRNA Anticodon
Amino…
Which of the three 20-amino-acid sequences listed below in the single-letter amino acid code is the most likely candidate to form a transmembrane region (α helix) of a transmembrane protein? Explain your answer.A. I T L I Y F G N M S S V T Q T I L L I SB. L L L I F F G V M A L V I V V I L L I AC. L L K K F F R D M A A V H E T I L E E S
Chapter 2 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
Ch. 2 - Suppose a chloride ion and a sodium ion are...Ch. 2 - Draw two different possible hydrogen-bonding...Ch. 2 - Prob. 3PCh. 2 - 4. What is the pH of each of the following...Ch. 2 - Prob. 5PCh. 2 - The weak acid HA is 2% ionized (dissociated) in a...Ch. 2 - 7. Calculate the pH values and draw the titration...Ch. 2 - What is the pH of the following buffer mixtures?...Ch. 2 - a. Suppose you wanted to make a buffer of exactly...Ch. 2 - Prob. 10P
Ch. 2 - You need to make a buffer whose pH is 7.0, and you...Ch. 2 - Describe the preparation of 2.00 L of 100 glycine...Ch. 2 - Carbon dioxide is dissolved in blood (pH 7.4) to...Ch. 2 - What is the molecular basis for the observation...Ch. 2 - The anno acid arginine ionizes according to the...Ch. 2 - It is possible to make a buffer that functions...Ch. 2 - A student is carrying out a biological preparation...Ch. 2 - Histidine is an amino acid with three titratable...Ch. 2 - Prob. 19PCh. 2 - A biochemical reaction takes place in a 1.00 ml...Ch. 2 - Is RNA-binding enzyme RNase A more likely to have...Ch. 2 - Consider a protein in which a negatively charged...Ch. 2 - Prob. 23PCh. 2 - Prob. 24P
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- 4.08 2.54 H H 1.02 1.02 1.67 E E = EXON = INTRON E 10.8 kbp 3.94 3.66 E = EcoRI site wwwwwwwww H = Hindill site HI Н 10.31t E E 1.76 1.10 Note: Fragment sizes are not to scale and all fragment lengths are in kilobase pairs (kbp) The a. Indicate what enzymes you would use for digestion and the gel electrophoresis pattern of the restriction fragments (draw a diagram of the gel with fragment positions, indicate field polarity, and direction of migration). Please do single and a double digest of the DNA. Grammarlyarrow_forwardIn the folded protein, His108 forms a salt bridge with Asp44. The pKa of the imidazole functional group in the side chain of histidine is 6.0. The pKa of the carboxylic acid functional group in the side chain of aspartate is 4.1. How do you think the pKa of the side chain of His108 will change in the folded protein? a. The pKa will be > 6.0. b. The pKa will be < 6.0. c. The pKa will not change. Use chemical reasoning to justify your answer.arrow_forwardAnswer a and barrow_forward
- Identify the type of mutation present in the CDS and discuss the implications on the protein.arrow_forward1₂ 4.08 H Note: 1.02 2.54 1.02 1.67 E E = EXON H = INTRON Î E 10.8 kbp 3.94 3.66 E = EcoRI site H = Hindill site HI 10.sht E E 1.76 1.10 Fragment sizes are not to scale and all fragment lengths are in kilobase pairs (kbp) Describe how you can determine if the gene is interrupted and, if so, the number of interruptions by restriction endonuclease analysis and Southern analysis. Iarrow_forwardPlease convert it to past tense and passive voice. Each group will be provided with two 20 g double-stranded DNA oligomers A and B in STE buffer (0.1M NaCl/ Tris/ 10 mM EDTA, pH 7.4). The sequence of the two oligomers used in this experiment is:5’ GCATTGCGCAGGGCCGAG 3’ (GC rich) 3’ AATGGTACGTATACTTTAT3’ (AT rich)In this experiment, you are going to identity oligomer samples A and B, GC or AT rich, by UV spectrophotometric method.1. Pipet 1 ml of each oligomer into a 1.5 ml Eppendorf tube and label the two tubes A and B.2. The absorption wavelength is 260 nm. Use STE buffer provided to set blank.3. You will be provided with two cuvettes. Use separate cuvette for each DNA sample.4. Transfer 1 ml of DNA sample A to cuvette and measure the UV absorbance at 260 nm (A260) atroom temperature. Repeat this step for Sample B.5. Transfer the DNA back to the original Eppendorf tube, close it and heat it to 45C for 7 minutes.6. Quickly transfer the sample from Eppendorf tube to cuvette, and…arrow_forward
- In a folded protein, Glu116 is close in three-dimensional space to Lys224. The pKa of the carboxylic acid functional group in the side chain of glutamic acid is 4.3. The pKa of the amino group in the side chain of lysine is 10.5. How do you think the pKa of the side chain of Glu116 will change in the folded protein? a. The pKa will be > 4.3. b. The pKa will be < 4.3. c. The pKa will not change. Use chemical reasoning to justify your answer.arrow_forwardI try to prepare for my biological chemistry exam, so I will appreciate if the answer is with some details. And I will be happy if there would be explanation for when I should use wich of the pka's. Thank you so much.arrow_forwardXylose racemase is a bacterial enzyme that converts the sugar D-xylose to L-xylose, which is needed in small amounts for the bacterial cell wall. The active site of xylose racemase includes a Y residue with a pKa = 7.2. The altered pKa of this residue, compared to its pKa in bulk water, is due largely to the presence of a nearby charged amino acid residue in the active site. Which is a likely explanation for the shift in the Y residue pka? The negative charge in a nearby E residue could stabilize a deprotonated Y residue. The negative charge in a nearby D residue could destabilize a protonated Y residue. The positive charge in a nearby K residue could stabilize a deprotonated Y residue. The positive charge in a nearby R residue could destabilize a deprotonated Y residue.arrow_forward
- It is estimated that the most common amino acid in a protein is leucine. What is the relative leucine frequency (in %) in the E. coli protein: NP_417192.1 (protein length: 750 aa)? (type only the numeric value two digits after decimal)arrow_forwardGiven the following DNA sequence: 3'-TACTTNGTNCTNTCN-5' where N stands for any nucleotide, give the complementary mRNA sequence. Indicate direction of strand as 3'--> 5' or 5'--> 3' as in the given sequence above. Give the amino acid sequence of your mRNA sequencelin No. 1. Indicate direction of strand as above. Use all lowercase letters, 3-letter name of amino acid separated by a hyphen (-), no spaces in-between.arrow_forwardFor each polypeptide derived in the following sequences: 5' CAA GAG GUA UCC UAC AGA 3' 5' GUC AUC UGG AGG GGC AUU 3' 5' CUA UGC AGU AGG ACA CCC 3' 1. Draw the structure of each polypeptide. 2. Label the amide bonds. 3. Identify the N-terminal and C-terminal amino acids. 4. Write the name of each polypeptide.arrow_forward
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