What is the major difference between motifs and domains?a) Motifs are unstable on their own, while domains are stable on their own.b) Motifs represent tertiary level of protein structure, while domains representquaternary level of protein structure.c) Motifs are made up of two or more of the same secondary structure elementscoming together, while domains are made up of two different secondarystructure elements coming together.d) All of the above are major differences between motifs and domains.e) None of the above are major differences between motifs and domains.

Motifs and domains are the structural elements of proteins that differ in their organisation and…

Answered: What is the major difference between…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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What following statement is TRUE concerning motifs and domains? a) Both motifs and domains are independently stable. b) Domains undergo dynamic individual changes that affect the entire protein c) B-a-ß loops, B barrels, and helix-turn-helix structure are types of domains d) Motifs and domains are part of secondary structural elements e) Ab initio computations predict motif folds accurately a majority of the time My guess is B.
1. Which best describes the contribution of primary (1’) structure of polypeptides to the native conformation of proteins: a) Structure that results from intrachain interactions of amino acid side chains b) Structure that results from interchain interactions of amino acid side chains c) Structure that results from base pairing d) Structure that results from the linear sequence of amino acids from beginning to end of molecule. 2. What shapes result from secondary structure: a) β- helix & α-sheets b) α-helix and β-sheets c) ɗ-bilayers & β-domains d) µ-folds 3. Which best describes the contribution of tertiary (3’) structure of to the native conformation of polypeptides and proteins: a) Structure that results from intrachain interactions of amino acid side chains b) Structure that results from interchain interactions of amino acid side chains c) Structure that results from base pairing d) Structure that results from the linear sequence of…
What type of interactions is primarily responsible for the creation of the following type of a) Covalent Bonding b) Ionic Interactions c)H-bonding d) Hydrophobic interactions structures? 1. a in the formation of a protein's primary structure 2. C in the formation of an alpha helix 3. d in the formation of a protein's tertiary structure 4. Which of the following polypeptides is capable of forming the most stable alpha helix? a) EEEEEE at pH 7 d) KKKKKK at pH 2 e) PPPPPP at pH 7 b) KKKKKKK at pH 7 (c) EEEEEE at pH 2 5/6. Explain your answer to the previous question. 7. Which of the following is NOT true of a collagen helix or collagen? a) A collagen helix cannot contain prolines. b) A collagen helix has a special amino acid called Hyp c) Collagen is a fibrous protein d) In collagen three helices come together to form a triple helix 8. Which of the following CANNOT make a H-bond. More than one can be circled. a) N-HO-C b) N…H-O-H Ⓒ)C=O....N-C d)C=O....H-O- 9. Which of the following…
What is the CORRECT way to classify the protein below according to its secondary- structure elements? un a) not possible to determine b) all a ○ c) alẞ Od) a + B e) all B
A sequence of amino acids in a certain protein is found to be -Ser-Gly-Pro-Gly-. The sequence is most probably part of a(n): A) parallel β sheet. B) α sheet. C) β turn. D) α helix. E) antiparallel β sheet.
Which of the following is primarily responsible for stabilizing the a-helix, a type of 1. secondary structure formed by a single nolvpeptide chain? hydrophobic interactions hydrogen bonds of backbone ionic interactions disulfide bridges hydrogen bonds involving the R-side chains a) b) atoms d) The atoms that make up the peptide bond that links amino acids together in a protein are in the same plane (coplanar). In the a-helix, how are these peptide bond planes arranged? 2. a) perpendicular to the a-helix approximately parallel to a-helix axis b) both parallel and perpendicular to the a-helix randomly oriented with respect to the axis of the a-helix peptide bond planes don't exist in the a-helix
Currently, aspartic acid is forming an ionic interaction with arginine in a protein. Part a) If arginine is replaced with glutamic acid, would the ionic interaction have its stability increased, decreased, or have no effect on the ionic interaction? Part b) If arginine is replaced with Lysine, would the ionic interaction have its stability increased, decreased, or have no effect on the ionic interaction? Part c) If arginine is replaced with isoleucine, would the ionic interaction have its stability increased, decreased, or have no effect on the ionic interaction?
Proper folding is essential for most proteins to function. Which of the following statement about protein folding are correct. There may be more than 1 right answer. a) changing the primary sequence will change the final conformation b) desaturation results in a protein that has a higher free energy than the native conformation c) protein spontaneously fold into their correct shape d) denatrutation will cause a protein to lose its tertiary structure
d) Describe what is meant by the primary structure of a protein? e) At the secondary level of structure, protein molecules will fold in either of two ways. • What are these two secondary forms of folding called? • What do these two forms look like structurally? • How is their structural arrangement stabilised? f) Describe the tertiary structure of a protein. g) Describe the biological function of the peptide hormone insulin. h) Haemoglobin is an example of a quaternary protein. Briefly describe the structure of this protein and state its biological function. Part 2 Monosaccharides and disaccharides are two of the sub-classes of Carbohydrates. Structure B shown below is a specific example of a monosaccharide. H HO Structure B CH₂OH H OH H OH H OH a) Name Structure B and describe its function within cells. b) State the name of a disaccharide that contains this molecule (Structure B) and describe its structure. c) A branched polysaccharide made up of many monomers of Structure B bonded…
d) Describe what is meant by the primary structure of a protein? e) At the secondary level of structure, protein molecules will fold in either of two ways. • What are these two secondary forms of folding called? • What do these two forms look like structurally? • How is their structural arrangement stabilised? f) Describe the tertiary structure of a protein. g) Describe the biological function of the peptide hormone insulin. h) Haemoglobin is an example of a quaternary protein. Briefly describe the structure of this protein and state its biological function.
Which of the following, if any, is correct about protein folding? a)2° structure formation is primarily entropic, 3° structure formation is primarily entropic b)2° structure formation is primarily entropic, 3° structure formation is primarily enthalpic c)2° structure formation is primarily enthalpic, 3° structure formation is primarily entropic d)2° structure formation is primarily enthalpic, 3° structure formation is primarily enthalpic e)None of the above
Which of the following types of molecular interactions play a role in protein folding? Select all that apply. A.)Hydrophobic interactions B.)Van der Waals attraction C.)Hydrogen bonds D.)Covalent bonds

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