BIOCHEMISTRY BOOKS ALC&MOD MST/ET PKG
1st Edition
ISBN: 9780134172507
Author: APPLING
Publisher: Pearson Education
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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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Students have asked these similar questions
The lipid portion of a typical bilayer is about 30 Å thick.
(a) Calculate the minimum number of residues in an a-helix required to
span this distance.
(b) Calculate the minimum number of residues in a B-strand required to
span this distance.
(c) Explain why a-helices are most commonly observed in transmembrane
protein sequences when the distance from one side of a membrane to the
other can be spanned by significantly fewer amino acids in a B-strand
conformation.
(d) The epidermal growth factor receptor has a single transmembrane helix.
Find it in this partial sequence:
.RGPKIPSIATGMVGALLLLVVALGIGILFMRRRH..
Explain how both alpha helices and beta sheets can be used by proteins that cross membranes.
Also explain what a hydropathy plot is and how such a plot can be used to differentiate transmembrane alpha helices from transmembrane beta sheets.
why do transmembrane proteins cross the phospholipid bilayer as an a-helix or B-barrel?
A. These structures arrange polar peptide bonds and hydrogen bonds to the exterior of the helix or barrel while nonpolar side chains are on the interior.
B. These structures sequester polar peptide bonds and hydrogen bonds to the interior of the helix or barrel
while nonpolar sidechains are on the exterior.
Chapter 10 Solutions
BIOCHEMISTRY BOOKS ALC&MOD MST/ET PKG
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
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- What can you infer about the structure and cellular localization of the protein below based on its hydropathy index? 40 -20 -40 20 40 60 80 100 120 140 160 180 200 220 240 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 indexarrow_forwardB) We also know from studies of protein structure that one turn of an a-helix includes 3.6 amino acid residues and extends the long axis of the helix by - 0.56 nm. Approximately how many amino acids must a helical transmembrane segment of an integral membrane protein have if the segment is to span the lipid bilayer defined by two stearate molecules laid end to end, plus the polar head groups to which the stearate molecules are attached (assume a polar head group has a diameter of 0.5 nm)?arrow_forwardMake a table with a scale of absorbance and the concentration of protein in Chromatin sample from the following data for excel graph Absorbance=660nm following data are of tubes with concern A =0 B=0.036 C=0.011 D=0.001 E=0.027 F=0.020 G=0.032 H1=0.176 H2=0.183 I1=0.150 I2=0.171 also plot the graph??arrow_forward
- An unspecified protein contains a 15-residue long α-helix with the following sequence: WEANIKQRLSTMGEYKQCHANG a. How many full turns are there in this α-helix? b. What is the length of the helix (in Angstroms) in the direction of the helix axis? c. How many hydrogen bonding interactions would be there in this α-helix? d. If it was a 310 helix instead with a helical pitch of 6 Å, is it long enough to span the 30 Å bilayer? Calculate and explain.arrow_forwardConsider 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-sheetarrow_forwardI'm honestly confused on where to start with this question. I think it has something to do with the residues per turn but can you please explain and show detailed work on the the problem. Researchers have discovered a new membrane protein that has three transmembrane domain αhelixes that span the lipid bilayer. a. If the lipid bilayer is 30 Å thick, what is the smallest number of amino acid residues that can be in each α-helixes for them to be long enough to span the bilayer? b. If one of the three α-helixes is titled at a 32° angle relative to an axis perpendicular to the surface of the lipid bilayer, what is the smaller number of amino acid helixes required for that helix to still span the lipid bilayer? c. How many hydrogen bonding interactions would there be in the smallest possible tilted transmembrane α-helix? d. If the tilted α-helix was a 310 helix instead how many amino acid residues would be required to span the lipid bilayer? How many amino acid residues would be required if…arrow_forward
- SDS-PAGE gels are used to study changes in protein primary structure. Which of the following statements about SDS-PAGE gels is correct? A. The negatively charged proteins will move towards the negatively charged electrode in the SDS-Page chamber B. A detergent is needed to disrupt protein secondary, tertiary, and quaternary structure before a gel can be run C. No "stains" or other treatments are needed to "see" the protein bands on a gel D. Long polypeptides move a further distance from the loading well in a SDS-PAGE gel than short polypeptidesarrow_forwardMonomeric, 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_forwardCreate a figure that includes a schematic of the topological map of AlaE. In your topological map, label; a. the cytoplasm, periplasm and membrane, b. the start and end of each predicted transmembrane helix with the residue letter and number found there, c. the N- and C-termini. The amino acid sequence is 149 in length: MFSPQSRLRHAVADTFAMVVYCSVVNMCIEVFLSGMSFEQSFYSRLVAIPVNILIAWPYGMYRDLFMRAARKVSPSGWIKNLADILAYVTFQSPVYVAILLVVGADWHQIMAAVSSNIVVSMLMGAVYGYFLDYCRRLFKVSRYQQVKAarrow_forward
- Alpha-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_forward-novel protein is described that functions best at pH 10.5, and contains a beta strand on one side. The authors report that at pH 10.5 this beta strand's interaction with an alpha helix is stabilized by an ionic interaction. a. Beneath each pair of amino acid names, draw out the structures for the two amino acids at pH 10.5 Asp-Arg Asn-Gln Cys-Glu b. Which of these pairs would be the best candidates for the ionic interaction at pH 10.5? (circle your choice): Asp-Arg Asn-Gln Leu-Gly C. Explain your choice in part b (25 words or less)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
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