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Chapter 9: Problem 11

What property enables the residues of the amino acids serine, threonine, and tyrosine to be phosphorylated? a. They are polar. b. They are non-polar. c. They contain a hydroxyl group. d. They occur more frequently in the amino acid sequence of signaling proteins.

Short Answer

Expert verified
c. They contain a hydroxyl group.

Step by step solution

01

- Understand the question

The question asks about the property that enables the residues of the amino acids serine, threonine, and tyrosine to be phosphorylated.
02

- Analyze the properties of each option

Consider each property:- Option a: Polar - Polar residues have an uneven distribution of charge.- Option b: Non-polar - Non-polar residues have an even distribution of charge.- Option c: Contains a hydroxyl group - A hydroxyl group (鈥揙H) is a functional group consisting of an oxygen atom bonded to a hydrogen atom.- Option d: More frequent in signaling proteins - Frequency in the sequence does not necessarily relate to the ability to be phosphorylated.
03

- Identify the relevant property for phosphorylation

For an amino acid to be phosphorylated, it must have a functional group that can be targeted by kinases. A common target is the hydroxyl group (鈥揙H), which is present in serine, threonine, and tyrosine.
04

- Select the correct answer

Based on the analysis, the ability to be phosphorylated is enabled by the presence of a hydroxyl group in their residues.

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

amino acid residues
Amino acid residues are the building blocks of proteins. When amino acids join together to form proteins, they link through peptide bonds. Each bond forms by removing a water molecule between an amino group's hydrogen and a carboxyl group's hydroxyl. This joining leaves a residual part of the amino acid integrated into the protein's structure. These residues retain the properties of the original amino acids. Understanding residues helps us predict protein behavior because each residue can interact with other molecules. Serine, threonine, and tyrosine residues play essential roles because they can be modified by phosphorylation.
hydroxyl group
The hydroxyl group (-OH) consists of an oxygen atom bonded to a hydrogen atom. This functional group is pivotal for many chemical reactions. Serine, threonine, and tyrosine have hydroxyl groups in their side chains, making them unique. One key characteristic of the hydroxyl group is its ability to form hydrogen bonds. This property increases the solubility of compounds in water. In the context of phosphorylation, the hydroxyl group is essential. Kinases transfer a phosphate group to the hydroxyl group during phosphorylation. The presence of this group in amino acid residues enables this critical modification.
protein phosphorylation
Protein phosphorylation is a crucial regulatory mechanism in cells. It involves adding a phosphate group to a protein by enzymes called kinases. This process typically occurs on serine, threonine, or tyrosine residues because of their hydroxyl groups. Phosphorylation changes the protein's structure and function. It can activate or deactivate enzymes, alter protein interactions, and signal pathways. This modification is vital in controlling various cellular processes, including metabolism, cell growth, and division. Understanding phosphorylation helps elucidate how cells respond to stimuli and maintain homeostasis.

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Most popular questions from this chapter

A doctor is researching new ways to treat biofilms on artificial joints. Which approach would best help prevent bacterial colonization of the medical implants? a. Increase antibiotic dosing b. Create implants with rougher surfaces c. Vaccinate patients against all pathogenic bacteria d. Inhibit quorum sensing

Why are ion channels necessary to transport ions into or out of a cell? a. Ions are too large to diffuse through the membrane. b. Ions are charged particles and cannot diffuse through the hydrophobic interior of the membrane. c. Ions do not need ion channels to move through the membrane. d. Ions bind to carrier proteins in the bloodstream, which must be removed before transport into the cell.

A scientist observes a mutation in the transmembrane region of EGFR that eliminates its ability to be stabilized by binding interactions during dimerization after ligand binding. Which hypothesis regarding the effect of this mutation on EGF signaling is most likely to be correct? a. EGF signaling cascades would be active for longer in the cell. b. EGF signaling cascades would be active for a shorter period of time in the cell. c. EGF signaling cascades would not occur. d. EGF signaling would be unaffected.

How does NF-kB induce gene expression? a. A small, hydrophobic ligand binds to NF-KB, activating it. b. Phosphorylation of the inhibitor Ik-B dissociates the complex between it and NF\(\mathrm{KB},\) and allows \(\mathrm{NF}-\mathrm{KB}\) to enter the nucleus and stimulate transcription. c. NF-kB is phosphorylated and is then free to enter the nucleus and bind DNA. d. NF-KB is a kinase that phosphorylates a transcription factor that binds DNA and promotes protein production.

Where do DAG and IP3 originate? a. They are formed by phosphorylation of cAMP. b. They are ligands expressed by signaling cells. c. They are hormones that diffuse through the plasma membrane to stimulate protein production. d. They are the cleavage products of the inositol phospholipid, PIP \(_{2}\)
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