Biochem 3.2   Protein Activity and Receptors Quiz

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Questions and Answers

What is the primary role of receptor proteins in cells?

  • To receive external signals and induce intracellular responses (correct)
  • To store energy for future use
  • To transport molecules across the cell membrane
  • To break down glucose for metabolism

What is the effect of an agonist on a receptor protein?

  • It permanently binds to the receptor and alters its structure.
  • It serves as a signaling molecule without binding.
  • It binds to the receptor and induces a biological response. (correct)
  • It blocks the receptor's activity and prevents responses.

How does the binding strength of an agonist to its receptor influence cellular response?

  • A stronger binding requires less agonist for a significant response. (correct)
  • A lower binding strength always leads to a higher cellular response.
  • Weakly binding agonists enhance receptor activity.
  • All agonists produce identical responses regardless of binding strength.

What is the characteristic of ligands called antagonists?

<p>They bind to receptors and prevent agonists from inducing a response. (C)</p> Signup and view all the answers

Which of the following describes a necessary condition for receptor protein activity?

<p>Binding of a specific ligand or agonist. (D)</p> Signup and view all the answers

What does a high Kd value imply about an agonist's binding to its receptor?

<p>The agonist requires larger amounts for a notable response. (A)</p> Signup and view all the answers

Which of the following factors can influence receptor protein activity?

<p>Feedback mechanisms from within the cell. (A)</p> Signup and view all the answers

What type of response is primarily induced by chemical signals acting through receptor proteins?

<p>Biological responses crucial for cell function (C)</p> Signup and view all the answers

In low-glucose conditions, how do cells typically respond?

<p>By breaking down stored glucose or using fat for energy. (B)</p> Signup and view all the answers

What does the G protein bind in its inactive form?

<p>Guanosine diphosphate (GDP) (C)</p> Signup and view all the answers

What occurs when an agonist binds to a GPCR?

<p>The GPCR undergoes a conformational change (A)</p> Signup and view all the answers

Which subunit of the G protein is responsible for interacting with enzymes when activated?

<p>α subunit (A)</p> Signup and view all the answers

What is the primary effect of insulin binding to its receptor on liver cells?

<p>Dephosphorylates phosphofructokinase-2 (D)</p> Signup and view all the answers

What is one of the most common effects of activated G proteins?

<p>Activation of adenylyl cyclase (D)</p> Signup and view all the answers

What happens to phosphoenolpyruvate carboxykinase (PEPCK) when insulin binds to its receptor?

<p>Its synthesis is reduced (B)</p> Signup and view all the answers

What is the result of the signal amplification phenomenon?

<p>A single agonist binding can lead to thousands of phosphorylated proteins (C)</p> Signup and view all the answers

What does the α subunit do to revert to its inactive form?

<p>Converts GTP to GDP (A)</p> Signup and view all the answers

How do hydrophobic signal molecules typically interact with target cells?

<p>By binding to cytosolic receptor proteins (B)</p> Signup and view all the answers

What type of proteins do GPCRs primarily interact with?

<p>G proteins (A)</p> Signup and view all the answers

What is the role of cytosolic receptors after binding to hydrophobic signals?

<p>Altering gene expression (D)</p> Signup and view all the answers

What effect does cortisol have compared to insulin in metabolism?

<p>Stimulates glucose production (D)</p> Signup and view all the answers

Which pathway is often triggered by GPCR signaling?

<p>MAP kinase pathway (B)</p> Signup and view all the answers

What is the primary role of cyclic AMP in cellular signaling?

<p>It serves as a second messenger (C)</p> Signup and view all the answers

Why do hydrophobic molecules require carrier proteins for transport in the bloodstream?

<p>They dissolve poorly in water (D)</p> Signup and view all the answers

What is a characteristic of G proteins?

<p>They are heterotrimers (C)</p> Signup and view all the answers

What is a key difference in response speed between cytosolic receptors and signal cascades?

<p>Cytosolic receptors activate existing proteins slowly (A)</p> Signup and view all the answers

What role does phosphofructokinase-2 play in glucose metabolism?

<p>It activates glycolysis (B)</p> Signup and view all the answers

Which of the following statements is true about the metabolic effects of insulin and cortisol?

<p>Insulin and cortisol have opposite metabolic effects (C)</p> Signup and view all the answers

What is the main way hydrophobic signals differ from other signaling methods?

<p>They do not often require transmembrane receptors (A)</p> Signup and view all the answers

What is the main difference in the effect of an agonist compared to an antagonist when binding to a receptor?

<p>An agonist causes a biological response, while an antagonist does not. (C)</p> Signup and view all the answers

How do antagonists generally interact with agonists at the receptor site?

<p>They prevent the agonist from binding when at the same site. (A)</p> Signup and view all the answers

What is an allosteric antagonist known to do?

<p>Reduce the affinity of the receptor for its agonist. (A)</p> Signup and view all the answers

What type of molecules primarily interact with transmembrane receptor proteins?

<p>Hydrophilic molecules that cannot easily cross the hydrophobic membrane. (A)</p> Signup and view all the answers

What occurs at the intracellular domain of a transmembrane receptor after an agonist binds the extracellular domain?

<p>The intracellular domain changes shape and alters its interactions. (D)</p> Signup and view all the answers

What is the result of secondary messenger activation due to agonist binding?

<p>Initiation of a biological response in the cell. (C)</p> Signup and view all the answers

What mechanism allows an agonist to counteract an antagonist?

<p>It can outcompete the antagonist for binding. (A)</p> Signup and view all the answers

What characterizes the binding of an allosteric antagonist compared to a competitive antagonist?

<p>Allosteric antagonists reduce the receptor's response without completely blocking agonist binding. (B)</p> Signup and view all the answers

Which statement accurately describes the role of secondary messengers?

<p>They amplify the signal from the activated receptor within the cell. (C)</p> Signup and view all the answers

In what situation would an increase in the concentration of an agonist not reverse the effects of an allosteric antagonist?

<p>When the antagonist binds at the allosteric site. (B)</p> Signup and view all the answers

Flashcards

Receptor Protein

A protein that receives an extracellular signal and triggers a specific response within the cell.

Ligand

A molecule that binds to a receptor protein and initiates a biological response.

Agonist

A ligand that binds to a receptor and triggers the intended biological response.

Kd (Dissociation Constant)

A measure of how tightly a ligand binds to its receptor. A smaller Kd indicates tighter binding.

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Antagonist

A ligand that blocks or prevents the binding of an agonist to its receptor.

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Cellular Responsiveness

The ability of a cell to respond to changes in its environment by altering its internal functions.

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Active Transport

The process by which a cell uses energy to bring molecules into the cell, often against their concentration gradient.

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Energy Management

A cell's ability to use stored energy or find alternative energy sources when the primary source is scarce.

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Glucose Breakdown

The process by which a cell breaks down stored glucose for energy.

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Glucose Storage

The process by which a cell stores excess glucose for later use.

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G Protein-Coupled Receptor (GPCR)

A type of receptor protein with seven transmembrane regions that interacts with G proteins.

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G Protein

A protein complex that activates various cellular processes, often by binding to GTP.

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Conformational Change

A change in protein shape or conformation, often triggered by ligand binding, leading to increased or decreased activity.

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GTP Hydrolysis

The process of converting GTP to GDP, returning the G protein to its inactive state.

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Adenylyl Cyclase

An enzyme that produces cyclic AMP (cAMP), acting as a second messenger in many signaling pathways.

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Signal Cascade

A chain of events that amplify a signal from a single agonist binding to a receptor, ultimately affecting the behavior of the cell.

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Phosphorylation

The process of adding a phosphate group to a protein, often changing its activity state.

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Primary Binding Site

The primary binding site on a receptor where an agonist typically binds.

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Allosteric Site

A binding site on a receptor that is different from the primary binding site. Binding to an allosteric site can affect the receptor's ability to bind the agonist or transmit its signal.

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Competitive Antagonist

A type of antagonist that binds to the primary binding site and directly prevents the agonist from binding.

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Allosteric Antagonist

A type of antagonist that binds to an allosteric site and indirectly affects the receptor's response to the agonist.

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Transmembrane Receptor

A type of receptor that spans the cell membrane, allowing communication between the extracellular environment and the cell's interior.

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Second Messenger

A molecule that is produced inside the cell in response to an agonist binding a transmembrane receptor. They transmit signals within the cell.

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Extracellular Domain

The region of a transmembrane receptor that extends outside the cell and binds to the agonist.

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Intracellular Domain

The region of a transmembrane receptor that extends inside the cell and interacts with intracellular pathways.

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Affinity

The ability of a receptor to bind to its agonist.

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Cytosolic Signaling

A type of cell signaling where the signaling molecule binds to a receptor inside the cell, rather than on the cell surface.

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Hydrophobic Agonist

A hydrophobic molecule that binds to a cytosolic receptor, triggering a cellular response.

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Cytosolic Receptor

A class of proteins that are located inside the cell and bind to hydrophobic signaling molecules.

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Nuclear Transport

The process where a cytosolic receptor, after binding a hydrophobic agonist, travels to the nucleus of the cell.

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Transcription Factor

Once in the nucleus, the cytosolic receptor binds to DNA and influences the expression of specific genes.

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Agonist Activation

The action of a signaling molecule in triggering its intended biological response.

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Dissociation Constant (Kd)

A measure of how tightly a molecule binds to its receptor.

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Extracellular Signal

A signaling molecule that activates a receptor on the cell surface.

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Study Notes

Protein Activity and Receptors

  • Proteins constantly adapt to cellular conditions, like responding to high glucose levels by storing or breaking down glucose for energy.
  • Receptor proteins receive extracellular signals (chemicals, light, electrical impulses, pressure) to trigger intracellular responses.
  • Ligands are chemical signals that bind to receptors, causing a response.
  • Agonists are ligands that bind receptors and induce primary responses; they have specific binding to their particular receptor. Similar molecules might also bind and induce responses.
  • Agonist binding strength is measured by Kd (dissociation constant); a low Kd indicates strong binding, allowing a significant response with lower agonist concentrations. Conversely, a high Kd indicates weak binding and requires higher agonist concentrations for a significant response.
  • Antagonists impede agonist binding; they don't elicit the same biological response of the agonist. Antagonists can bind at the same or different sites as agonists, either competing for the binding site or interfering with the agonist's ability to transmit a signal or reduce the affinity between the receptor and agonist.
  • Allosteric antagonist binding can hinder agonist binding but not completely block it. They might reduce the receptor's affinity for the agonist or change the intensity of the response.

Transmembrane Receptors

  • Hydrophilic signals can't pass through the cell membrane directly.
  • Transmembrane receptors receive them; the extracellular domain binds the signal, triggering a conformational change in the intracellular domain.
  • This change alters interactions with other molecules within the cell, triggering a response.

G Protein-Coupled Receptors (GPCRs)

  • GPCRs are a crucial class of transmembrane receptors.
  • They have seven transmembrane regions and interact with G proteins, which are protein complexes that mediate intracellular signaling.
  • In an inactive state, the G protein binds GDP; agonist binding changes the receptor, causing GDP to switch to GTP, activating the G protein.
  • The activated G protein subunits then interact with other enzymes (like adenylyl cyclase in the case of cAMP production), influencing downstream events and triggering cellular responses (e.g., changes in gene expression).

Signal Cascades

  • Signal cascades can amplify initial signals, leading to a larger cellular response via a series of protein phosphorylations.
  • A single agonist binding can lead to the phosphorylation of numerous proteins.
  • This process is called signal amplification.

Hydrophobic Signals and Cytosolic Receptors

  • Hydrophobic signals readily cross the cell membrane.
  • They interact with cytosolic receptors, and the resulting receptor-ligand complex then enters the nucleus.
  • In the nucleus, the complex acts as a transcription factor affecting gene expression (e.g., regulates glucose production).

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