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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4. You're working on a structure of a protein and its folding. You think that the interaction between Asp123 and Arg29 is important in determining the structure of the protein. a) What type of amino acid is Asp (acidic, basic, hydrophobic, or polar)? b) What type of amino acid is Arg (acidic, basic, hydrophobic, or polar)? c) What is the strongest interaction that can form between Asp123 and Arg29? You create a mutant Arg29> Lys d) What type of amino acid is Lys (acidic, basic, hydrophobic, or polar)? e) Would you expect this substitution mutation to cause major folding problems? Why or why not? You create mutant Arg29> Glu you discover that this mutant is unable to fold properly, so the protein is nonfunctional. f What type of amino acid is Glu (acidic, basic, hydrophobic, or polar)? g) How does this amino acid substitution cause the protein to fold incorrectly? You find another mutant that also as the same Arg29> Glu mutation. However, this mutant protein įs able to fold normally.…
Let’s suppose we have downloaded the structure of Hemoglobin from PDB. Now we want to retrieve the location of helices and loops in it. How can we do it? How can we depict a protein’s coordinate info in a modeling program? (Subject: Bioinformatics)
Consider a short peptide with the sequence M-C-Q-L-Y-P-E-D-K. List the ionizable groups in this peptide, and the net charge of the whole peptide at pH a) 1.5, b) 7.0, and c)12.0.
In standard nomenclature, peptide sequences are read out in which direction? a) C to N b) 3’ to 5’ c) N to C d) 5’ to 3’
Hemoglobin has two alpha-type chains and two beta-type chains. This would be a description of: a) primary structure b) secondary structure c) tertiary structure d) quaternary structure Myoglobin has much helix-turn-helix motif. This would be a description of: a) primary structure b) secondary structure c) tertiary structure d) quaternary structure Myoglobin folds up into a ball-like structure. This would be a description of: a) primary structure b) secondary structure c) tertiary structure d) quaternary structure Domains differ from subunits in that: a) subunits are connected by peptide bonds while domains are not b) domains are connected by peptide bonds while subunits are not c) subunits are larger than domains d) subunits are hydrophobic while domains are hydrophilic
Which of the following describes a primary protein structure?A) Protein structure maintained by disulfide linkages.B) Amino acid sequence maintained by peptide bonds.C) Protein chains maintained by interactions of peptide backbones like an α-helix.D) Arrangement of multiple protein subunits.E) Protein structure maintained through multiple hydrogen bonds.
Write the anticodons for the following amino acids: a) Met b) Trp c) Ser d) Leu
What general structural feature is shared by proteins that specifically form homodimers (but not homotrimers, homoteramers etc)? Only one answer is correct. the surface consists of hydrophilic alpha-helix. the surface is highly modified by post-translational modification. the surface is permanently bound by chaperones. the surface is unstructured. the surface, or part of it, is self-complementary.
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.
3)Which of the following statements are true? Choose all that apply a)There are multiple codons possible for nearly all amino acids b)Each stop codon also codes for an amino acid c)Each tRNA will base pair with only one codon d)The start codon also codes for an amino acid e)Each codon in mRNA codes for exactly one amino acid f)Each codon in tRNA codes for exactly one amino acid g)Each anticodon in tRNA pairs with exactly one codon h)Each tRNA carries exactly one type of amino acid
What protein structure is represented in either panel of the figure above? Question 11 options: a) Quaternary b) Secondary c) Tertiary d) Quinary e) Primary

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