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 10, Problem 4P
The lipid portion of a typical bilayers is about
a. Calculate the minimum number of residues in an
b. Calculate the minimum number of residues in an
c. Explain why
d. The epidermal growth factor receptor has a single transmembrane helix. Find it in this partial sequence:
...RGPKIPSIATGMVGALLLLVVALGIGILFMRRRH…
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What can you infer about the structure and cellular localization of the protein below based on its hydropathy index?
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Residue number
A. It is a cytosolic protein
B. It is a lysosomal enzyme that works in the lumen of the lysosome.
O C. It is a cytosolic protein with a single-pass transmembrane domain
O D. It is a multi-pass transmembrane protein that will be ultimately found on the cell surface but may also be found In the ER, Golgi, or
lysosomal membranes.
Hydropathic index
The engineered peptide in this RIP is designed to bond to certain proteins in the plasma membrane of skin cancer cells. Based on the data discussed here, what might you suspect about the structure of human skin cancer cells?
A. They contain unique membrane proteins not commonly found in other types of human cancer cells
B. Their membrane structure is identical to some other types of human cancer cells
Consider a protein with the following amino acid sequence:
--R-V-G-M-A-E-I-Q–V–L-K-F-V-I-H-L-
Which would be the most likely structure of the protein? Justify your answer.
a. An a-helix with B-turn
b. A parallel B-sheet
c. An antiparallel B-sheet
Chapter 10 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
Ch. 10 - Prob. 1PCh. 10 - Given these molecular components--glycerol, fatty...Ch. 10 - The classic demonstration that cell plasma...Ch. 10 - The lipid portion of a typical bilayers is about...Ch. 10 - In the following situations, what is the free...Ch. 10 - Propose an experiment that would distinguish...Ch. 10 - Prob. 7PCh. 10 - Peptide hormones (such as insulin) must bind to...Ch. 10 - Prob. 9PCh. 10 - Prob. 10P
Ch. 10 - Prob. 11PCh. 10 - Prob. 12PCh. 10 - Prob. 13PCh. 10 - Prob. 14PCh. 10 - The concentration of glucose in your circulatory...Ch. 10 - ATP is synthesized from ADP, Pi , and a proton on...Ch. 10 - The Na+/ glucose symport transports glucose from...Ch. 10 - Prob. 18PCh. 10 - Prob. 19PCh. 10 - The transport of aspirin (pKa = 3.5, structure...Ch. 10 - Prob. 21P
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Monomeric, single-pass transmembrane proteins span a membrane with a single a helix that has characteristic chemical properties in the region of the bilayer. Which of the three 20-amino-acid sequences listed below is the most likely candidate for such a transmembrane segment? O TLIYFGVMAGVIGTILLIS O ITPIYFGPMAGVIGTPLLIS ITEIYFGRMAGVIGTDLLISarrow_forwardAlpha-helices have 3.6 amino acid residues per turn, ie a helix 36 amino acids long would form 10 turns, and The axial distance between adjacent residues is 3.5 Angstroms. Beta-helices have two residues per repeat unit which gives the beta-strand a 7 Angstrom pitch. This compares with the alpha-helix where the axial distance between adjacent residues is only 1.5 Angstroms. Then how many residues in an alpha-helix conformation would it take to traverse the same distance as 10 residues in beta-strand conformation?arrow_forwardThe major reason that antiparallel beta-stranded protein structures are more stable than parallel beta-stranded structures is that: Select one: a. parallel ones are in a slightly less extended configuration than antiparallel strands. b. parallel ones do not have as many disulfide crosslinks between adjacent strands. c. parallel ones do not stack in sheets as well as antiparallel strands. X d. parallel ones have fewer hydrogen bonds than antiparallel strands. e. parallel ones have weaker hydrogen bonds between adjacent strands.arrow_forward
- Non covalent bonds are very important in cell biology, could you explain why and provide an example that illustrates their importance ( do not chose protein folding as an example) What are the different levels of protein structure and what are the different parameters (sequence, type of bonds, etc...) that influence protein folding at these different levels?arrow_forwardWhich of the following statements are correct? explain your answers.A. An individual ribosome can make only one type of protein.B. All mRNAs fold into particular three-dimensional structures that are required for their translation. C. the large and small subunits of an individual ribosome always stay together and never exchange partners.D. ribosomes are cytoplasmic organelles that are encapsulated by a single membrane.E. Because the two strands of DNA are complementary, the mRNA of a given gene can be synthesized using either strand as a template.F. An mRNA may contain the sequence ATTGACCCCGGTCAA.G. the amount of a protein present in a cell depends on its rate of synthesis, its catalytic activity, and its rate of degradation.arrow_forward81. You have used the primary amino acid sequence of a newly identified protein (of unknown function) to make a hydropathy plot. From this plot you believe it might be a transmembrane receptor. This is because the plot tells a. the secondary structure is likely made up of several B sheets. b. the secondary structure is likely made up of a-helices. c. the protein would be readily hydrolyzed if in an aqueous environment. d. on average, there are a lot of hydrophobic amino acids in the protein. e. there are several hydrophobic areas interspersed with short hydrophilic stretches. you that 82. You are studying a mutant type of garter snake known for its odd slithering movement. You isolated the mutated gene and this morning you just got the results from your DNA sequencing. What would be your first step towards determining the potential function of the protein encoded by this gene? a. Use X-ray crystallography to determine the tertiary structure of the protein. b. Use computer programs that…arrow_forward
- Many transmembrane proteins have a large series of hydrophobic amino acids such as those in the middle of the protein (around b). Why would this make sense, and where would you expect these to be located in the final protein structure?arrow_forwardA Ramachandran Plot illustrates acceptable phi (φ) and psi (ψ) angles for amino acids in a polypeptide. What is the primary factor that restricts these angles? The relative abundance of proline. a The degree of side chain (R-group) interactions. b The relative amount of inter- and intra-strand hydrogen bonding. c Solvent entropy (hydrophobic effect) d Steric hindrance.arrow_forwardConsider the following DNA sequence:CATGTGTAGTCTAAAa. Write the sequence of the DNA strand that would be repli-cated from this one.b. Write the sequence of the RNA molecule that would betranscribed from the DNA strand.c. State how many codons the sequence specifies.d. State how many amino acids the sequence specifiesarrow_forward
- With regard to the 30-nm fiber, a key difference between the solenoidand zigzag models isa. the solenoid model suggests a helical structure.b. the zigzag model suggests a more irregular pattern of nucleosomes.c. the zigzag model does not include nucleosomes.d. Both a and b describe key differences between the models.arrow_forwardIntegral membrane proteins can exist as all of the following, except: a. A single helix b. A beta barrel A single beta strand d. A group of seven helices C.arrow_forwardb. What is the difference between the 3' and the 5' ends of a nucleotide chain? C. Do the chains run the same way? d. How are the chains connected? e. Which bases bond to each other? f. What kinds of bonds hold the chain together? 3. What are the main differences between RNA and DNA? 4. Distinguish between the structure of pyrimidines and purines. Explain why adenine bonds only to thymine. 5. Name the five nitrogenous bases in the table below, and put an X in the correct column for each base. Then indicate if the base if found in DNA (D), RNA (R), or both (B) hparrow_forward
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