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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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 amino acids from beginning to end of molecule
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?
……….. proteins do not have a defined secondary structure composition. They can have both helices and sheets. When primary sequence is studied, it does not look like there is any order in the sequence, but there is order in 3D structure. ……… amino acids are clustered in the core of the protein, away from the solvent (water molecules) and …….. amino acids are on the surface of the protein.
1. Search for the `P06858` a) Give information about the PTM and Processing of this protein. b) Which position has maximum amount of variations? Give details about the variations. (Eg: What kind of variation? Feature ID? Disease association? etc..)
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.…
2. Identify the structural level in each protein. A) quaternary structure B) tertiary structure C) secondary structure D) primary structure 1) The protein folds into a compact structure stabilized by interactions between R groups. 2) the combination of two or more protein molecules to form an active protein 3) B-pleated sheet 4) the peptide bonds betwecen the amino acids 5) the structural level achieved when hydrogen bonds form between the carboxyl group of one amino acid and the amino group of a different amino acid
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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’
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.
6. Given: 3"--TACTTCAAACCGGGCCCGATT--5 a) Give the sequence of nucleotides in the mRNA. b) What is the sequence of amino acids in the protein coded by the MRNA? c) If the first G is substituted by A, what is the sequence of amino acids in the protein? d) What type of mutation is illustrated by (e)?
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.

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