Answered: The tertiary structure of…

The tertiary structure of immunoglobulin G is composed of 12 discrete: A. alpha-helices B. collapsed beta-barrel domains C. parallel beta-sheets D. helix-turn-helix domains

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter4: Organization Of The Cell

Section: Chapter Questions

Problem 8TYU: All of the following are true of integrins except (a) they are receptor proteins (b) they help...

See similar textbooks

Related questions

Q: Protein structure and function: a) Name two common post-translational modifications of proteins in…

A: Protein is one of three macro nutrients, which are supplements the body needs in bigger amounts. The…

Q: In fact, immunoglobulin G consists of two identical copies of the heavy chain and two identical…

A: Immunoglobulin (Ig) are also considered as antibodies, which is a glycoprotein. These are produced…

Q: 5a) Draw this peptide at the physiological pH (7.4) with the following 1-letter codes: F-R-I-D-A-Y…

A: Proteins are composed of amino acids. They are linked together by peptide linkages. Proteins have…

Q: We now have at least three SARS-CoV-2/COVID-19 vaccines approved by the FDA for use in the United…

A: The vaccines are: 1. Pfizer-BioNTech – Authorized on December 11, 2020 2. Moderna – Authorized on…

Q: A mixture of proteins with the following properties were purified using cation exchange…

A: Cation exchange chromatography is a technique that separates proteins based on their net surface…

Q: The FDA finds that chickens across the US are infected with a new type of bird-flu. They determine…

A: A gene is a DNA-based functional heredity unit that delivers instructions for the production of RNA…

Q: 21. Which protein structure is most consistent for the hydropathy graph of the intrinsic membrane…

A: Hydropathy graph depicts the hydrophobicity and hydrophilicity of a polypeptide chain based on the…

Q: 18. The following is correct regarding calmodulin: A) It is a widespread calcium-responsive protein.…

A: Calmodulin It is a small, highly conserved intermediary protein. It constitutes about 148 amino…

Q: 87) For a the viral proteins a. If the viral protein is made in the RER, it will go back to the…

A: Proteins are composed of amino acids, which are bound together by peptide linkage. Amino acids…

Q: Your friend's genetic test revealed that they have a rare mutation - they lack the glycotransferase…

A: A medical procedure that replaces blood lost from injury, surgery, or illness is a blood…

Q: Propose a protocol (~100 words) to study the efficacy of the antibody in this mouse model.

A: According to the given data, factor 801A is transduction molecule essential for growth of ovarian…

Q: below One common structure found in "folded" SSRNA is a • Using the RNA base abbreviations: A, G, C…

A: Stem-loop is the structure formed by single-stranded RNA (ribonucleic acid) when nucleotides base…

Q: You are analyzing the peptide ala-ile-glu-lys-phe-val- tyr-cys. If you treat the peptide with…

A: Hi! Thank you for the question, as per the honor code, we are allowed to answer the first…

Q: The new E484K mutation in SARS-CoV Spike produces a) a change from a hydrophillic to a hydrophopic…

A: The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a new coronavirus associated…

Q: Imidazole is used to elute His6-tagged proteins from Ni-NTA resins because imidazole is: a.…

A: On the Ni-NTA column the protein that is His-tagged bind to the column with high affinity. The…

Q: An American biochemist Erwin Chargaff discovered that in the cells of all organisms he studied, the…

A: Introduction :- All living things are made up of cells, which are the basic building blocks. There…

Q: 76) Nuclear localization signal can be a. Simple sequence in which we have a stretch of acidic amino…

A: A nuclear localization signal (NLS) is an amino acid pattern that 'marks' a polypeptide for nuclear…

Q: 2. (6) Examine the two proteins labelled a) and b). Which of the two Ramachandran plots, c) or d) is…

A: Amino acids are backbone of proteins or polypeptide chains. When amino acids joined covalently…

Q: True or False: An IgM monomer can bind as many as 10 epitopes?

A: ADAPTIVE IMMUNE SYSTEM:- This system is a combination of two:- Lymphocytes and antigen-presenting…

Q: Classify the symmetrical arrangement of the subunits (e.g., C2 , C3 , D 2 , helical, icosahedral).…

A: Symmetry is a property of some biological molecules and structures that describes how they are…

Concept explainers

Proteins

We generally tend to think of proteins only from a dietary lens, as a component of what we eat. However, they are among the most important and abundant organic macromolecules in the human body, with diverse structures and functions. Every cell contains thousands and thousands of proteins, each with specific functions. Some help in the formation of cellular membrane or walls, some help the cell to move, others act as messages or signals and flow seamlessly from one cell to another, carrying information.

Protein Expression

The method by which living organisms synthesize proteins and further modify and regulate them is called protein expression. Protein expression plays a significant role in several types of research and is highly utilized in molecular biology, biochemistry, and protein research laboratories.

Question

12) The tertiary structure of immunoglobulin G is composed of 12 discrete:

A. alpha-helices

B. collapsed beta-barrel domains

C. parallel beta-sheets

D. helix-turn-helix domains

Expert Solution

This question has been solved!

Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.

This is a popular solution!

SEE SOLUTION Check out a sample Q&A here

Step 1

VIEW

Step 2

VIEW

Trending now

This is a popular solution!

Step by step

Solved in 2 steps

SEE SOLUTION Check out a sample Q&A here

Knowledge Booster

Learn more about

Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.

Similar questions

1. "Interferons (IFNs)‐α and ‐β are expressed in response to a virus infection and are released from the cell in which they are produced. IFNs induce an antiviral state in other neighboring cells. a. Which cellular process is inactivated when IFN‐treated cells are infected with a virus? b. One arm of the IFN‐induced antiviral state is the synthesis of 2′,5′‐oligoA in response to viral infection. In one sentence or a simple diagram, what is the effect of this on the cell? c. Another arm of the IFN‐induced antiviral state is activation of the protein kinase in response to viral infection. In one sentence or a simple diagram, what is the effect of this on the cell? d. All cells contain the genes for IFNs. IFN synthesis is stimulated by virus infection. Would you expect a cell that has been treated with IFN to synthesize IFN in response to a viral infection? Explain your answer."
In fact, immunoglobulin G consists of two identical copies of the heavy chain and two identical copies of the light chain. However, the early researchers did not know the exact number of chains or how they were arranged. Draw a simple diagram of an alternative quaternary structure for immunoglobulin G, showing how the heavy and light chains might be arranged and connected by disulfide bonds to form a structure with a total molecular mass of 150,000.
Antibodies are effective against bacteria as well as viruses, but some bacteria produce an enzyme that cuts immunoglobulin G molecules right at the “bend” to separate each antigen-binding “arm” from the “stem.” (a) What type of bond is broken by the bacterial enzyme and what type of reaction does this enzyme catalyze? (b) Would the action of the bacterial enzyme affect the ability of immunoglobulins to cross-link bacterial cells?.
18. The following is correct regarding calmodulin: A) It is a widespread calcium-responsive protein. B) It is present in all eukaryotic groups (animals, plants, fungi, protistans, etc.). C) It is a cytoplasmic protein that alters the activities of a broad range of other proteins. D) A homodimer, a holoprotein of calmodulin will bind a total of four Ca2+ ions. E) All of the above Answer: Explanation:
1. The T conformation of hemoglobin is stabilized (in part) by a hydrogen bonding interaction between the negatively-charged carboxylate group of the side chain of Asp99 in the β-subunit of one αβ dimer and the -OH group of the side chain of Tyr42 in the α-subunit of the opposing αβ dimer. Draw a diagram of this hydrogen bonding interaction (show complete side chains). 2. In an abnormal hemoglobin variant known as Hemoglobin-Radcliffe, the Asp99 residues in the β-subunits are replaced by alanine residues. This change eliminates the hydrogen bonding interaction that normally occurs between Asp99 in the β-subunit of one αβ dimer and Tyr42 in the α-subunit of the opposing αβ dimer. a) What effect would you expect this change to have on the quaternary structure and oxygen binding properties of hemoglobin? (see question 1) b) Draw a diagram to illustrate the difference in the oxygen binding curves that would be obtained with normal hemoglobin and Hemoglobin-Radcliffe.
1) What is an obvious physical difference between an immunoglobulin (an antibody) and glucose (a monosaccharide)? 2) Draw a sketch of a method that could be used to separate immunoglobulins from glucose utilizing the physical differences between the molecules that you mentioned in question 1.
1. The human hemoglobin molecule, like all mammalian he- moglobins, is comprised of two a-chains and two ß-chains con- ₂ taining 141 and 146 amino acid residues, respectively. Be- cause the molecule possesses two-fold symmetry, there are a1-a2, B1-B2, and a1-B2 interfaces formed by amino acid sidechains through which structural changes are transmitted underlying ligand binding. The most important of these is the a1-B2 interface that is illustrated in the diagram on the right. All of the sidechain interactions across the a1-B2 interface are hydrophobic except for that between Asp(a94) and Asn- (B102). This is the only polar interaction across the α1-³2 in- terface and it helps to stabilize the oxy- or R-conformation. Its approximate location in the Hb molecule is represented by the red double arrow in the diagram on the right. His FG4 97 Asp G1 (99) Tyr C7 (42) Hb mutant (a) T State (deoxy) 95 The C6 41 (a) The diagram below on the right-hand side illustrates the polar Asp(a94). . . Asn…
a) 5'-ATGGGCTCGCACTCATAA-3' b) 5'-ATGGTCTCGAACTCATAA-3' c) 5'-ATGGGCTCGAACTCATAA-3' d) 5'-ATGGGCTCGAACACATAA-3' e) 5'-ATGGGCTCGAATTCATAA-3' Excuse me, the answer you shows to me is not appear in the five options.
7
What do x-helices and B-sheets have in common? Jay A) The length of the 10-amino acid x-Helix and B-sheet strand will be the same. OB) Both are stabilized by glycine and proline residues. C) Both are stabilized by hydrogen bonding involving carbonyl oxygens and amide nitrogens. OD) The same amino acids stabilize both forms of secondary structure.
The figure below shows amino acid interactions between the a /B2 subunit interface of hemoglobin. These interactions stabilize the T state of the protein. Based on the figure below, which amino acid in the picture below, if replaced with glutamate, would decrease the Ka of hemoglobin for O2 the most? Include both the residue and the residue number in your response (For example, V1 or K127). to B, V34 8- a, R141 D126 K127 Noncovalent
All of the following are true of integrins except (a) they are receptor proteins (b) they help organize the cytoskeleton (c) they are part of the ECM (d) they are important in cell signaling (e) they are located in the plasma membrane