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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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 α-helix required tospan this distance.
(b) Calculate the minimum number of residues in a β-strand required to span this distance.
(c) Explain why α-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 aβ-strand conformation.
(d) The epidermal growth factor receptor has a single transmembrane helix. Find it in this partial sequence: . . . RGPKIPSIATGMVGALLLLVVALGIGILFMRRRH . .
Make 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??
If Kd= 100 nM, [RNA] = 10 nM, and [protein] = 1 uM
a) What fraction of RNA is bound?
b) What fraction of protein is bound?
c) What is the concentration of the protein:RNA complex?
d) Is it reasonable to assume that total protein = free protein?
e) Is it reasonable to assume that total RNA = free RNA?
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
- A segment of DNA has the followimg sequence of bases.. 5'-ATGCAATGATATTGAAGCTTA-3' a) What sequence of bases would appear in mRNA transcribed from this segment? b) Assume the first base in this mRNA is the beginning of a codon. What order of amino acid would be translated into a polypeptide synthesized along this segment? c) Give anticodons for each tRNA associated with the translation in part (b)arrow_forwardAn 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_forwardWhen a protein denatures in a cell, it tends to assemble into aggregates. Propose an explanation for this phenomenon. Briefly describe a disease that is caused by aggregation of denatured proteins.arrow_forward
- Why is a b-barrel as opposed to a b-sheet optimal for a transmembrane protein? Think about the energetics specifically.arrow_forwardWhich 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 Sarrow_forwardwhat does it mean to say that trends in a double helix is antiparallel? A. They each have a sugar-phoshate backbone. B. They each have a 5'-3' directionality (or polarity). C. They have opposite directionalty in terms of relative positions of 5' and 3' ends.arrow_forward
- Consider the following in light of the concept of levels of structure (primary, secondary, tertiary, quaternary)as defined for proteins.(a) What level is shown by double-stranded DNA?(b) What level is shown by tRNA?(c) What level is shown by mRNA?arrow_forwardMany 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_forwardShown below are two cartoon views of the small globular protein StrepG inwhich an α helix is packed against a four-strand β sheet. The sheet is madeup of two “β-hairpins” (a β-hairpin is a “β-turn-β” structure). Refer to theimages and answer the questions that follow: (a) Identify the locations of the N- and C-termini of StrepG.(b) Indicate the orientation of the helical macrodipole, showing the (δ+)and (δ-) ends of the macrodipole.(c) How many residues are in the helix?(d) Do you predict that the α helix and β sheet are amphiphilic or not?Briefly explain.(e) The following two peptides are part of the primary sequence of StrepG.Based on your answer to part (d), which one is more likely to correspondto the α helix? Which is most likely to be part of a β-hairpin? Explainyour choice.Peptide #1: DAATAEKVFKQYAND or Peptide #2: VDGEWTYDDATKTFTVarrow_forward
- The usual hydrophobic region of a membrane is around 30 Angstroms. Knowing this, about many amino acid residues would a transmembrane helix have?arrow_forwardexplain how a hydropathy plot can distinguish proteins with single transmembrane domains from those with multiple transmembrane domainsarrow_forwardUse a rough diagram to compare the structures of a proteina-helix and an antiparallel b-sheet. For simplicity, showonly the backbone atoms of the protein.arrow_forward
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