Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 30, Problem 11P
Interpretation Introduction
Interpretation:
The reason for existence of two subunit structures of ribosomes rather than a large single-subunit entity needs to be explained.
Concept Introduction:
Ribosomes are termed as protein builders of the cell. They connect to the one amino acid at a time to form long chains. They are found in both prokaryotic and eukaryotic cells thus they are special cell organelle.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Can you suggest a reason why ribosomes in all living organisms consist of two subunits and not one supramolecular complex?
The dimensions of prokaryotic ribosomes are approximately 14 nm by 20 nm. If ribosomes occupy 20% of the volume of a bacterial cell, calculate how many ribosomes are in a typical cell as E. coli. Assume that the shape of a ribosome is approximately that of a cylinder.
1. Integral and peripheral membrane proteins employ multiple strategies to keep them associated to a biological
membrane. View these three proteins below, and for each protein shown, answer the following questions:
A) What type of membrane protein is this? Integral, peripheral, monotopic, polytopic? How do you know?
Justify your label by features of the protein shown in the image.
B) Describe the overall tertiary structure of each protein. Be certain to mention hydrophilicity/hydrophobicity
of the surfaces of this protein.
C) Provide a detailed description of how each protein is held associated to the biological membrane.
Protein 2
Protein 3
Protein 1
"H,N.
Exterior
Cytosol
Chapter 30 Solutions
Biochemistry
Ch. 30 - Prob. 1PCh. 30 - Prob. 2PCh. 30 - The Second Genetic Code Review the evidence...Ch. 30 - Codon-Anticodon Recognition: Base-Pairing...Ch. 30 - Consequences of the Wobble Hypothesis Point out...Ch. 30 - Prob. 6PCh. 30 - Prob. 7PCh. 30 - Prob. 8PCh. 30 - Prob. 9PCh. 30 - The Consequences of Ribosome Complexity Eukaryotic...
Knowledge Booster
Learn more about
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
- The Consequences of Ribosome Complexity Eukaryotic ribosomes are larger and more complex than prokaryotic ribosomal. What advantages and disadvantages might this greater ribosomal complexity bring to a eukaryotic cell?arrow_forwardFull length resilin that is not in a cell is thought by some to form a tertiary structure of this form (picture attached) The yellow portions represent exon 1 and the blue portions exon 3. These structures assemble into a kind of lattice or network. In full length resilin, stress in the form of mechanical pressure or heating to remove water results in a tighter network that excludes any water internally. How might this behavior of resilin produce its ‘elasticity’? Explain how the looser water containing structure and the tighter water excluding structure may give us a mechanism for the elasticity.arrow_forwardI am studying pancreatic islet cells and have isolated, cloned, and sequenced a novel protein that you postulate has 4 transmembrane segments. Name and explain two methods I could use to reconstitute a lipid bilayer to study the function of the transmembrane protein in vitro.arrow_forward
- Create a ROUGH SKETCH (no need for exact hydropathy indices and residue numbers) of the hydropathy plot for the given membrane protein. -coo Please follow the color assignment of the helical domains and properly label the plot and axes. Here is an example: Amino Outside terminus Transmembrane helices are predicted by hydrophobic stretches of 20-25 aa residues 10 50 100 150 200 250 Hydrophobic Inside Hydrophilic Carboxyl terminus -3 10 50 100 150 200 250 Residue number Bacteriorhodopsin Hydropathy indexarrow_forwardBiological membranes are critical components of cells that allow compartmentalisation of cellular contents. The diagram shows a biological membrane comprised of a lipid bilayer with a single polypeptide integrated into the membrane and spanning the membrane seven times. What types of amino acids are likely present in the parts of the polypeptide chain labelled 1-7 and in the parts of labelled A-G? What is the name of the effect that forces the polypeptide to arrange itself like this within the lipid bilayer? Give an example of a type of molecule that can move freely across the lipid bilayer and explain why it can do so based on its chemical properties.arrow_forwardWhile investigating structure-function studies in a membrane transport protein, a researcher discovered a single nucleotide mutation that led to the loss of a key alpha-helical segment of the protein in the hydrophilic domain. The mutation that led to this finding is most likely which of the following? Hint: helix breaker O AUC to GUC GAG to CCU GUU to GCU GUG to UUG O CUC to CCCarrow_forward
- 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_forwardBacteriorhodopsin is an integral membrane protein containing 248 amino acids. X- ray analysis of this protein reveals that it consists of seven parallel a-helical segments, each of which traverses the bacterial cell membrane. Calculate the minimum number of amino acid residues necessary for a single a-helical segment to completely traverse the bacterial cell membrane (assume the membrane has a thickness of 4.1 nm). (a) (b) Estimate the fraction of the bacteriorhodopsin protein that is involved in membrane-spanning helices.arrow_forwardNon 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_forward
- Which of the following (could be more than one) would not be a rational explanation for why the three-dimensional structure of a protein is driven and stabilized largely by noncovalent rather than covalent bonds?a) Proteins may be degraded for energy, and if their three-dimensional structures were heldtogether by mostly covalent bonding, this might be too difficult to accomplishb) Proteins will need to be unfolded to cross biological membrane, and if their three-dimensionalstructures were held together by mostly covalent bonding, this might be too difficult toaccomplish.c) Protein function (transport, enzyme catalysis, etc...) may require flexibility in the three-dimensional structure to allow for conformational change, and if protein three-dimensionalstructure were held together by mostly covalent bonding, this might be too difficult toaccomplish.d) All of the answer choices are rational explanations for why the three-dimensional structure of protein is driven and stabilized largely…arrow_forwardPolypeptides which are normally synthesized in the endoplasmic reticulum are about20 amino acids longer when they are synthesized by ribosomes not attached to the endoplasmicreticulum, What is the significance of this increase in length?arrow_forwardThe 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..arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningBiology: The Unity and Diversity of Life (MindTap...BiologyISBN:9781305073951Author:Cecie Starr, Ralph Taggart, Christine Evers, Lisa StarrPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Biology: The Unity and Diversity of Life (MindTap...
Biology
ISBN:9781305073951
Author:Cecie Starr, Ralph Taggart, Christine Evers, Lisa Starr
Publisher:Cengage Learning
The Cell Membrane; Author: The Organic Chemistry Tutor;https://www.youtube.com/watch?v=AsffT7XIXbA;License: Standard youtube license