Which of the choices are types of posttranslational modifications a newly synthesized protein may undergo? Select all the choices that apply. changes to hydrogen bonding capabilities formation of an amide bond between Cys and an isoprenyl group removal of prosthetic groups removal of the thiol group from a Cys residue modulation of charges on amino acids proteolytic cleavage covalent attachment of oligosaccharides to Asn, Thr, or Ser

Which of the choices are types of posttranslational modifications a newly synthesized protein may undergo? Select all the choices that apply. changes to hydrogen bonding capabilities formation of an amide bond between Cys and an isoprenyl group removal of prosthetic groups removal of the thiol group from a Cys residue modulation of charges on amino acids proteolytic cleavage covalent attachment of oligosaccharides to Asn, Thr, or Ser

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

See similar textbooks

Related questions

Q: (c) Outline how you would investigate whether BCMAP would be an effective inhibitor for the protein…

A: Inhibitors are the molecules that slow down or completely block the protein activity of molecules,…

Q: Glycosylation is a major type of protein post-translational modification. Identify the amino acid…

A: Cavalent or generally enzymatic reactions takr place after or during translation are termed as post…

Q: Long-range interactions between residues on a single polypeptide chain are classified as quaternary…

A: Proteins are the linear chain of amino acids attached together via peptide bonds. Proteins are…

Q: When answering the questions below, please use the one-letter code for the amino acid, with NO…

A: Acid hydrolysis: Acid hydrolysis of any protein/polypeptide is being used to detect amino acids…

Q: The following peptide that has been acetylated at the C-terminus: CH3C(O)-GEEGH-NH2 Plot the…

A: Titration is a very useful procedure to estimate the concentration of any unknown compound in a…

Q: Here is a putative peptide sequence (position number on top of residues): 1 2 3 4 5 6 7 8 9 10 11…

A: Hi! Thanks for your question. As you have posted multiple sub-parts, we are answering only the first…

Q: Imagine the main chain of a protein bends back on itself, so that two amino acid residues R, and R,…

A: Salt bridge is a bond between amino acids which carry opposite charges. The opposite charges exert…

Q: Calculate the pl of the amino acid using the titration curve. 04 pH 0 6 8 SO 10 O 12.0 12 10.0 8.0…

A: Pi is the isoelectric point. This is the pH at which the Amino acid carries no net charge. The…

Q: When performing his experiments on protein refolding, Christian Anfinsen obtained a quite different…

A: Anfinsen showed that the protein folding data resides within the amino acid sequence of the protein.…

Q: The following data describe the catalysis of cleavage of peptide bonds in small peptides by the…

A: Peptide bond cleavage is the basic process of hydrolysis of a polypeptide where the peptide bond…

Q: Changing one amino acid within a protein sequence from a tryptophan to a stop codon would be best…

A: Mutation is the change in the nucleotide sequence of the DNA that causes a change in the mRNA.…

Q: Describe your first proposed step clearly in words (1-2 sentences) including the buffer/pH used.…

A: Proteins are biomolecules, that is compose of amino acids linked by the peptide bonds. Each protein…

Q: Draw the Ala-Ser-Leu-Asp polypeptide (perspective formula) showing the fully extended backbone…

A: Proteins are folded peptides. Peptides are polymers made up of amino acid residues linked via a…

Q: Which of the following sequences represents a recognition site for N-linked glycosylation where X is…

A: N-linked glycosylation, is the attachment of an oligosaccharide, sometimes also referred to as…

Q: A protein has been sequenced after cleavage of disulfide bonds. The protein is known to contain 3…

A: Proteins are macromolecules formed by amino acids. A total of 20 different amino acids exist in…

Q: A) Can you please tell me which of these A.A have a negative side chain? Names of choices in picture…

A: Amino acids are biomolecules that have an amino group, a hydrogen atom, an R group and a carboxyl…

Q: Which of the following statements about the post-translation modification of proteins by…

Q: why do you think this is? In your explanation, you should describe the specific molecular…

A: 1. Proline is rarely found in beta sheets or alpha helices this is because proline is totally…

Q: In the protein adenylate kinase, the C-terminal region has the sequence Val-Asp-Asp-Val-Phe-…

A: A helical wheel representation is a type of plot or visual representation used to illustrate the…

Q: Two proteins are discovered, and both are shown to have a potential in treating fatty liver…

A: There are few points fatty liver syndrome . These are as follows : We know that fatty liver…

Q: detail how cation exchange chromatography works and what you would use to elute your target protein.…

A: Cation exchange chromatography is a technique used to separate proteins based on their net surface…

Q: Once the chains of peptides that make up lysyl-tRNA synthetase protein are synthesized in ribosomes,…

A: Protein folding is the process where the proteins fold themselves to come to their native form. This…

Q: Throughout the polypeptide chain, must the amino acid residues at the active site be next to one…

A: A polypeptide chain is a lengthy sequence of amino acids that contains amino acid residues that…

Q: This image is showing the conformations of ubiquitin superimposed. What do the structures in this…

A: Ubiquitin is a regulatory protein and it plays pivotal role in protein homeostasis in our body. It…

Question

Which of the choices are types of posttranslational modifications a newly synthesized protein may undergo? Select all the
choices that apply.
changes to hydrogen bonding capabilities
formation of an amide bond between Cys and an isoprenyl group
removal of prosthetic groups
removal of the thiol group from a Cys residue
modulation of charges on amino acids
proteolytic cleavage
covalent attachment of oligosaccharides to Asn, Thr, or Ser

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

Follow-up Questions

Read through expert solutions to related follow-up questions below.

Follow-up Question

Which of the choices are types of posttranslational modifications a newly synth
choices that apply.
changes to hydrogen bonding capabilities
formation of an amide bond between Cys and an isoprenyl group
removal of prosthetic groups
removal of the thiol group from a Cys residue
modulation of charges on amino acids
proteolytic cleavage
covalent attachment of oligosaccharides to Asn, Thr, or Ser
Incorrect
< Feedback
Macmillan Learning
There are four correct choices.
Proteolysis (proteolytic cleavage) is the
partial or complete breakdown of a
protein. Keep in mind that amino acids
are linked together during
protein synthesis.
Recall that some proteins are
posttranslationally modified to form
glycoproteins. Consider the structure,
or components of, a glycoprotein.
In addition, think about how the
methylation of a protein affects
intramolecular forces.

Solution

by Bartleby Expert

SEE SOLUTION

Similar questions

One of the most common features of anion binding sites is the presence of an a-helical structure. Using a schematic diagram of a helix, describe what you've observed. The direction of the dipole and the N-terminus of the helix should be clearly indicated. Show the (general) base structure of the glutamic acid functional group side chain.
You are presented with Cytidine 5' triphosphate and Thymidine 5' triphosphate. Draw and upload to Efundi these phosphorylated structures as they would be connected in a polinucleotide in the order CpT / Show the individual phosphorylated structures first then show how they combine to form the polynuleotide. Show at any one of these structures where the glycosidic bond occurs
Consider the phenolic hydroxyl group of a particular Tyr residue in a protein. Suppose the hydroxyl group in the unfolded protein in aqueous solution, where the group is exposed to H2O, has a pKa of 10.0. If that group is found in a hydrophobic environment in the interior of the protein when the protein is folded into its native tertiary structure, would you expect the pKa of the phenolic hydroxyl to be higher or lower in the folded protein interior than in H2O? Explain your reasoning.
Small molecules are used as inhibitors of protein action - as drugs. They most often do this by blocking the active site within the protein. Potential drugs can be screened computationally to determine if they are strongly bound to the protein. Figure 1 shows a possible conformation of a candidate drug molecule, 4-bromo-2- carboxymethylamide-pyrrole (abbreviation: BCMAP) at the active site of a protein (abbreviation: PR). Figure 2 shows the full protein structure whilst figure 3 shows a known inhibitor of the protein at the site, overlayed with another calculated conformer of BCMAP. (a) Explain what types of interactions, both intermolecular and intramolecular, that a molecular mechanics forcefield must be able to describe in order to be able to accurately determine the geometry of BCMAP in the protein. Identify which interactions will be the most important to describe accurately. Figure 1.4-bromo-2-carboxymethylamide-pyrrole (BCMAP) (C, N, O, and Br atoms in yellow, blue, red, and…
A schematic diagram of the helical structure of cytochrome b562 is reproduced below. Thisprotein belongs to the family of -proteins that have a four-helix bundle. Number the helices 1 – 4according to their N  C direction. Indicate relative orientations of the macrodipoles of helices 1 – 4adjacent to the diagram of cytochrome b562. Remember that according to the definition of a dipolethat the arrow points towards the positive end.
The biosynthetic pathway for the two amino acides E and H is shown schematically in the Figure below: A W E 2 Z H How would this pathway change if C was mutated and non-functional?
In posttranslational modification, phosphates are attached to which 3 amino acids? - tyrosine - serine - proline - lysine - threonine
The folding of intrinsically disordered proteins is prevented by the presence of Ser, Lys, and Glu residues. What do these amino acids have in common? Why do they disrupt IDPs?
Can you please describe the specific components that each of these structures are comprised of ( alpha helices and beta sheets) in more detail? Also, what do the different colors represent? Your reply will be greatly appreciated. The ligand that was assigned to me is tadalafil.
Posttranslational modifications of proteins do not include: peptide bond formation glycosylation acetylation of N-terminal peptide bond cleavage disulfide bond formation QUESTION 16 14 15 16 streptomycin puromycin 17 18 19 20 Which one of the following antibiotics does NOT function by interfering with the translational/post-translation process tunicamycin penicillin O tetracyclin O O
Given the following diagram of how protein AWESOME1 binds to it's target DNA, describe the potential effects of each of the 5 mutations shown below. The wild-type sequence of a helix #1 is also shown in the blue box, and all the mutations are in helix #1 (see numbers for identifying particular residues). a helix #1 R(1)-V-I-L-Y-F-W-I-M-Y-F-S-H-Y-W-R(16) #1 Predict the consequence of the following mutations: 1) Arg(1) to Glu 2) Arg(1) to Ala 3) Phe(6) to lle 4) Trp(7) to Phe 5) Met(9) to Pro in