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Protein Structure and Function Quiz
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Protein Structure and Function Quiz

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Questions and Answers

What is the significance of HCl in protein metabolism during digestion?

HCl denatures proteins, making them more accessible to proteolytic enzymes, and activates pepsinogen into pepsin for protein breakdown.

Identify three key biological roles of proteins and provide an example for each.

Proteins serve in catalysis (enzymes), transport (hemoglobin), and mechanical support (collagen).

What are proteolytic enzymes, and how do they contribute to protein metabolism?

Proteolytic enzymes, such as pepsin and trypsin, break down proteins into smaller peptides and amino acids, facilitating nutrient absorption.

Briefly describe the process of metabolism with respect to anabolism and catabolism.

<p>Metabolism encompasses all biochemical reactions; anabolism builds complex molecules from simpler ones, while catabolism breaks down molecules for energy.</p> Signup and view all the answers

Mention a clinical disorder associated with protein metabolism and its implication.

<p>Phenylketonuria (PKU) is a disorder resulting from a deficiency in the enzyme phenylalanine hydroxylase, leading to the accumulation of phenylalanine.</p> Signup and view all the answers

What are the structural differences between globular and fibrous proteins?

<p>Globular proteins have a coiled shape with hydrophobic amino acids inside, while fibrous proteins consist of long, parallel chains linked by disulphide bridges.</p> Signup and view all the answers

Explain the role of enzymes as globular proteins in metabolism.

<p>Enzymes catalyze metabolic reactions, facilitating the breakdown and transformation of substances in the body.</p> Signup and view all the answers

Identify the primary function of collagen in the body.

<p>Collagen provides structural support and tensile strength in bones, cartilage, tendons, and ligaments.</p> Signup and view all the answers

How does protein digestion begin in the stomach?

<p>Protein digestion starts when dietary protein stimulates the secretion of gastrin, increasing hydrochloric acid (HCl) production in the stomach.</p> Signup and view all the answers

What are zymogens and their purpose in protein digestion?

<p>Zymogens are inactive precursors of peptidases that prevent autodigestion and are activated in the intestinal lumen.</p> Signup and view all the answers

Describe the three phases of protein digestion.

<p>The three phases of protein digestion are gastric (in the stomach), pancreatic (in the small intestine), and intestinal (also in the small intestine).</p> Signup and view all the answers

What role does nitrogen play in amino acid metabolism?

<p>Nitrogen, obtained from dietary proteins, is metabolized and excreted from the body as urea and ammonia.</p> Signup and view all the answers

What is the significance of hydrophilic amino acids being exposed on globular proteins?

<p>The exposure of hydrophilic amino acids allows globular proteins to be soluble in aqueous environments, facilitating their biological functions.</p> Signup and view all the answers

What role does HCl play in gastric digestion?

<p>HCl reduces the pH of the stomach to 1-2, acting as both an antiseptic agent and a denaturating agent for proteins.</p> Signup and view all the answers

How is pepsin activated and what is its function?

<p>Pepsin is activated from pepsinogen in the acidic gastric environment and functions as an endopeptidase, hydrolyzing peptide bonds involving Phe, Tyr, Trp, and Met.</p> Signup and view all the answers

List the key endopeptidases found in pancreatic juice and their importance.

<p>The key endopeptidases include Trypsin, Chymotrypsin, and Elastase, crucial for the digestion of proteins in the small intestine.</p> Signup and view all the answers

What is the function of bicarbonate secreted by the pancreas during digestion?

<p>Bicarbonate raises the intestinal pH to optimum levels for pancreatic enzyme activity, which is around pH 8.</p> Signup and view all the answers

Differentiate between endopeptidases and exopeptidases.

<p>Endopeptidases cleave internal peptide bonds within a protein, while exopeptidases cleave terminal peptide bonds, releasing free amino acids or dipeptides.</p> Signup and view all the answers

What specific amino acids do trypsin and chymotrypsin preferentially cleave?

<p>Trypsin preferentially cleaves at arginine and lysine residues, while chymotrypsin targets aromatic amino acids.</p> Signup and view all the answers

How are di- and tri-peptides processed after absorption in enterocytes?

<p>Di- and tri-peptides are hydrolyzed into free amino acids within the enterocyte after absorption.</p> Signup and view all the answers

What stimulates the secretion of pancreatic juice?

<p>The secretion of pancreatic juice is stimulated by the peptide hormone cholecystokinin.</p> Signup and view all the answers

How are dipeptides and tripeptides processed after entering mucosal cells?

<p>They are immediately hydrolyzed into single amino acids.</p> Signup and view all the answers

What is the primary route of absorption for amino acids in the small intestine?

<p>Amino acids are absorbed via sodium-dependent secondary active transport.</p> Signup and view all the answers

What consequence can arise from the paracellular absorption of larger protein molecules?

<p>It can lead to immune responses and food allergies due to immunogenic reactions.</p> Signup and view all the answers

What clinical condition is caused by the immune response to gluten, and what is its effect on the small intestine?

<p>Celiac disease results in immune-mediated damage to the small intestine.</p> Signup and view all the answers

What initiates the process of acute pancreatitis related to protein digestion?

<p>Premature activation of trypsinogen within the pancreas initiates autodigestion.</p> Signup and view all the answers

What results from a deficiency in pancreatic secretion regarding protein digestion?

<p>It leads to incomplete digestion and absorption of fats and proteins.</p> Signup and view all the answers

How are free amino acids released from enterocytes into the portal system?

<p>Free amino acids are released through sodium-independent transporters on the basolateral membrane.</p> Signup and view all the answers

Explain the significance of energy in the absorption process of amino acids within the small intestine.

<p>The absorption process is energy-requiring, utilizing ATP for carrier-mediated transport.</p> Signup and view all the answers

Study Notes

Protein Structure and Function

  • Proteins are nitrogenous organic compounds composed of amino acid chains linked by peptide bonds.
  • There are 20 common amino acids, each with a unique R group.
  • Proteins have diverse biological roles, including catalysis (enzymes), transport (hemoglobin), storage (myoglobin), motion (actin and myosin), support (collagen), protection (antibodies), and regulation (hormones).
  • Globular proteins are coiled, with hydrophobic amino acids inside and hydrophilic ones outside, making them soluble and involved in metabolic reactions. Examples include enzymes and hemoglobin.
  • Fibrous proteins have long parallel chains linked by disulfide bridges, providing structural strength. Examples include keratin and collagen.

Protein Metabolism

  • Metabolism comprises anabolism (synthesis) and catabolism (breakdown).
  • Nitrogen enters the body through dietary amino acids and leaves as urea, ammonia, and other metabolites.
  • Protein digestion involves three phases: gastric, pancreatic, and intestinal.

Gastric Digestion

  • Cooking denatures proteins, making them easier to digest.
  • Gastrin stimulates HCl secretion, lowering stomach pH to 1-2.
  • HCl acts as an antiseptic and denatures proteins.
  • Pepsin, an endopeptidase, hydrolyzes peptide bonds involving specific amino acids (Phe, Tyr, Trp, Met).

Pancreatic Digestion

  • Pancreatic juice contains endopeptidases (trypsin, chymotrypsin, elastase) and carboxypeptidase.
  • These are secreted as inactive zymogens to prevent autodigestion.
  • They are serine proteases with serine residues in their active sites.
  • Optimal pH is 8, maintained by bicarbonate secreted in response to secretin.
  • Cholecystokinin stimulates pancreatic juice secretion.
  • Endopeptidases cleave internal peptide bonds, while exopeptidases (carboxypeptidases, aminopeptidases) cleave terminal bonds.
  • Trypsin targets arginine and lysine residues; chymotrypsin targets aromatic amino acids; elastase targets hydrophobic amino acids.

Intestinal Digestion and Absorption

  • Final digestion yields free amino acids, dipeptides, and tripeptides.
  • Di- and tripeptides are absorbed and hydrolyzed within enterocytes.
  • Amino acids are transported into portal blood via sodium-dependent and -independent transporters.
  • Most globular proteins are completely hydrolyzed, but some fibrous proteins (e.g., keratin) are only partially digested.

Clinical Significance

  • Food allergies can result from the absorption of partially digested proteins.
  • Celiac disease is an immune response to gluten, damaging the small intestine.
  • Acute pancreatitis arises from premature trypsinogen activation within the pancreas.
  • Pancreatic insufficiency (e.g., due to chronic pancreatitis, cystic fibrosis, or pancreatectomy) impairs fat and protein digestion and absorption.

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Description

Test your knowledge on the structure and functions of proteins, including their biological roles and metabolism. This quiz covers the different types of proteins, such as globular and fibrous proteins, as well as the process of protein metabolism.

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