Protein Structure and Function Quiz
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Questions and Answers

What are the building blocks of proteins?

Amino acids

What does a side chain dictate?

The function of that amino acid

What type of bond links amino acids together?

Peptide bonds

What is the term for 10 or more amino acids bonded together?

<p>Polypeptide</p> Signup and view all the answers

Nonessential amino acids are required in the diet.

<p>False</p> Signup and view all the answers

Essential amino acids are produced by the body.

<p>False</p> Signup and view all the answers

Which of the following are examples of branched chain amino acids involved in maintaining muscle tissue? (Select all that apply)

<p>Valine</p> Signup and view all the answers

What are limiting amino acids, and where are they typically found?

<p>Limiting amino acids are the essential amino acids found in the smallest quantity in foods. They are often found in cereals (lysine and threonine) and legumes (methionine and cysteine).</p> Signup and view all the answers

What are conditionally essential amino acids, and why are they important?

<p>Conditionally essential amino acids are usually synthesized by the body, but they can become essential under certain conditions, such as illness or stress. They are therefore important for maintaining adequate protein synthesis during these times.</p> Signup and view all the answers

What are some of the physiologic functions of proteins? (Select all that apply)

<p>Tissue growth and maintenance</p> Signup and view all the answers

What is the primary function of protein in the body?

<p>The primary function of protein is to supply material for the growth and maintenance of body tissues.</p> Signup and view all the answers

Describe the difference between anabolism and catabolism.

<p>Anabolism is the process of building up new cellular material from smaller components, whereas catabolism is the breakdown or destruction of body tissues.</p> Signup and view all the answers

How much nitrogen is provided by 6.25 grams of protein consumed?

<p>1 gram of nitrogen</p> Signup and view all the answers

What is nitrogen balance, and what are the different types?

<p>Nitrogen balance is the difference between nitrogen intake and nitrogen excretion. It has three different types: nitrogen equilibrium, where intake and loss are equal, negative nitrogen balance, where more nitrogen is excreted than consumed, and positive nitrogen balance, where intake exceeds excretion.</p> Signup and view all the answers

What is the role of proteins in enzyme production?

<p>Proteins are essential for manufacturing enzymes, which are proteins that exist in all cells of living things. They accelerate biochemical reactions necessary for digestion and metabolism.</p> Signup and view all the answers

Enzymes are catalysts for biochemical reactions.

<p>True</p> Signup and view all the answers

Enzymes are specific to their substrates and reactions.

<p>True</p> Signup and view all the answers

What is the role of proteins in hormone production?

<p>Proteins are necessary for manufacturing hormones, which are chemicals synthesized in the body that act as messengers or signals to control various physiological processes.</p> Signup and view all the answers

Give an example of how proteins are involved in hormone regulation.

<p>Proteins are components of thyroid hormones, which regulate metabolic rate and cellular development, and insulin and glucagon, which maintain stability of blood glucose concentrations.</p> Signup and view all the answers

What is a buffer, and how do proteins act as buffers?

<p>A buffer is a compound that helps stabilize fluids and tissues by maintaining a constant pH level. Proteins act as buffers by releasing or accepting hydrogen ions to counteract any pH changes, helping to maintain a stable internal environment.</p> Signup and view all the answers

What is oncotic pressure, and how does it affect fluid balance?

<p>Oncotic pressure is the effect of proteins on fluid balance. Proteins in blood vessels attract water, creating a pressure that pulls fluid from surrounding tissues back into the capillaries, maintaining proper blood volume and preventing edema, or swelling.</p> Signup and view all the answers

What is edema?

<p>Edema is swelling that occurs due to an accumulation of fluid in tissues. It can result from inadequate protein intake, which reduces oncotic pressure and allows fluid to leak into tissues.</p> Signup and view all the answers

Proteins are involved in the immune response by producing antibodies to attack antigens.

<p>True</p> Signup and view all the answers

Each antibody is specific to a particular antigen.

<p>True</p> Signup and view all the answers

The body keeps a record of the characteristics of each antibody manufactured, allowing it to produce the same antibodies more quickly in the future.

<p>True</p> Signup and view all the answers

When do proteins provide a source of energy?

<p>Proteins provide a source of energy during times of inadequate energy supply from fats and carbohydrates.</p> Signup and view all the answers

Depletion of lean body tissue can occur when the body breaks down muscle for energy.

<p>True</p> Signup and view all the answers

What is the importance of adequate intake of all macronutrients?

<p>Adequate intake of all macronutrients, including proteins, fats, and carbohydrates, is essential for optimal health and to prevent the depletion of lean body tissue that can occur from relying solely on protein for energy.</p> Signup and view all the answers

What happens to proteins in the stomach during digestion?

<p>In the stomach, hydrochloric acid (HCL) denatures proteins by breaking some of the bonds that hold them together. This process prepares the proteins for further breakdown.</p> Signup and view all the answers

What is the role of the enzyme pepsin in protein digestion?

<p>HCL activates the enzyme pepsin, which further breaks down remaining bonds in the proteins, reducing them to smaller polypeptides and some free amino acids.</p> Signup and view all the answers

Where do polypeptides and free amino acids go after being partially digested in the stomach?

<p>After partial digestion in the stomach, polypeptides and some free amino acids are emptied into the small intestine for further digestion.</p> Signup and view all the answers

How do partially digested proteins elicit the release of regulatory peptides?

<p>Partially digested proteins in the small intestine trigger the release of regulatory peptides.</p> Signup and view all the answers

What is the function of proenzymes in protein digestion?

<p>Proenzymes are inactive forms of enzymes that are activated in the small intestine. They further degrade polypeptides and amino acids, completing the process of protein digestion.</p> Signup and view all the answers

What happens after intestinal degradation of proteins?

<p>After intestinal degradation, some small peptides and free amino acids are used by intestinal cells for energy and synthesis of other compounds, while the remaining amino acids are transported into the liver.</p> Signup and view all the answers

What is the role of the liver in amino acid metabolism?

<p>The liver monitors the amount of amino acids absorbed and adjusts the rate of their metabolism, ensuring that the body has the right balance of amino acids for various needs.</p> Signup and view all the answers

Deamination is the process by which nitrogen is removed from a substance.

<p>True</p> Signup and view all the answers

The body converts ammonia to urea for excretion by the kidneys.

<p>True</p> Signup and view all the answers

What is the function of the carbon skeleton remaining after deamination?

<p>The remaining carbon skeleton after deamination can be used for energy or to make other substances.</p> Signup and view all the answers

What is transamination?

<p>Transamination transfers nitrogen from one chemical group to another without forming ammonia.</p> Signup and view all the answers

What is protein turnover?

<p>Protein turnover is a continuous process where proteins are constantly synthesized and degraded.</p> Signup and view all the answers

Describe the formation of an amino acid pool during protein turnover.

<p>During protein turnover, new amino acids mix with existing amino acids in the body, forming an amino acid pool.</p> Signup and view all the answers

What is the significance of a stable amino acid pool in protein turnover?

<p>A stable amino acid pool allows for the efficient use of these amino acids to make other compounds, ensuring that the body has a sustainable source of amino acids for various functions.</p> Signup and view all the answers

What factors are assessed in protein quality?

<p>Protein quality is assessed based on its composition and digestibility, which determine how well the protein provides the necessary building blocks for the body.</p> Signup and view all the answers

What is the Protein Digestibility Corrected Amino Acid Score (PDCAA)?

<p>PDCAA, also known as biological value, measures protein quality based on its composition and digestibility.</p> Signup and view all the answers

What is the difference between complete and incomplete proteins?

<p>Complete proteins contain all essential amino acids in adequate amounts, while incomplete proteins lack one or more essential amino acids.</p> Signup and view all the answers

Give examples of sources for complete and incomplete proteins.

<p>Complete proteins are found in animal sources like meat, poultry, fish, eggs, and dairy products, and plant sources like soy. Incomplete proteins are typically found in plant sources like beans, lentils, grains, and nuts.</p> Signup and view all the answers

Describe complementary proteins.

<p>Complementary proteins are proteins from different sources that combine to form a complete protein, providing all essential amino acids when consumed together.</p> Signup and view all the answers

What is the RDA for protein in adults aged 19-70?

<p>The RDA for protein in adults aged 19-70 is approximately 0.8 grams per kilogram of body weight per day.</p> Signup and view all the answers

Infants, children, and pregnant women require slightly higher protein intakes than adults.

<p>True</p> Signup and view all the answers

What is an inborn error of metabolism, and give an example.

<p>An inborn error of metabolism is an inherited defect in the way a certain substance is metabolized. Phenylketonuria (PKU) is an example, caused by a deficiency in the phenylalanine hydroxylase enzyme.</p> Signup and view all the answers

Describe the dietary implications for individuals with phenylketonuria (PKU)?

<p>Individuals with PKU must follow a strict diet that is low in phenylalanine, limiting high-protein foods and relying on special phenylalanine-free supplements for additional protein, micronutrients, and energy.</p> Signup and view all the answers

What is the impact of stress induced by critical injury on nitrogen balance?

<p>Stress induced by critical injury can lead to accelerated tissue breakdown, resulting in negative nitrogen balance and loss of body mass.</p> Signup and view all the answers

Which of the following conditions necessitate elevated protein intake? (Select all that apply)

<p>Brain injury</p> Signup and view all the answers

Higher protein intake is needed during recovery from severe burns.

<p>True</p> Signup and view all the answers

Why does certain types of kidney or liver failure necessitate reduced protein intake?

<p>Certain types of kidney or liver failure make the body unable to effectively metabolize proteins, reducing the intake can help alleviate the burden on these organs.</p> Signup and view all the answers

Describe protein malnutrition and what it leads to.

<p>Protein malnutrition occurs when there is insufficient intake of nitrogen-containing foods, leading to a deficiency in protein, affecting various bodily functions.</p> Signup and view all the answers

What are the characteristics of Kwashiorkor?

<p>Kwashiorkor is a form of protein malnutrition characterized by adequate energy intake but insufficient protein intake, often seen in children from underdeveloped countries after weaning from breast milk. Symptoms include edema, hair discoloration, and altered skin pigmentation.</p> Signup and view all the answers

What are the characteristics of marasmus?

<p>Marasmus is a form of malnutrition characterized by inadequate consumption of energy combined with compromised protein status, often observed in underdeveloped countries where food sources are scarce, individuals with wasting diseases causing significant weight and muscle loss, and the elderly population. Symptoms include dry or loose skin, hair discoloration, severe tissue loss, and delayed development.</p> Signup and view all the answers

What are the general steps involved in treating malnutrition?

<p>Treatment for malnutrition typically involves identifying the underlying cause and formulating interventions to address it. It also focuses on ensuring adequate intake of protein and energy to correct nutritional deficiencies and support recovery.</p> Signup and view all the answers

Study Notes

Lecture Objectives

  • Classify amino acids and proteins
  • Describe the physiological function of proteins
  • Explain protein metabolism
  • Detail dietary protein recommendations
  • Identify inborn errors of metabolism
  • Recognize malnutrition

Protein Structure and Composition

  • Proteins are major structural components of all cells, maintaining shape
  • Composed of nitrogen, carbon, hydrogen, and oxygen
  • May also contain phosphorus, sulfur, iodine, or iron

Amino Acids

  • Building blocks of proteins
  • Chemical structure includes a hydrogen (H), amino group (NH2), and an acid group (COOH) attached to a central carbon (C)
  • Side chain (R group) determines the specific function of the amino acid
  • Side chains may be hydrophobic (non-polar, repelling water) or hydrophilic (polar, attracted to water) and carry electrical charges
  • Interactions with other amino acids include hydrogen bonding and electrostatic forces

Protein Structure

  • Amino acids combine in a specific sequence to form a protein, forming the primary structure
  • Chains of ten or more amino acids are called polypeptides
  • Proteins are large polypeptides

Essential vs. Nonessential Amino Acids

  • Nonessential amino acids: the body can synthesize them
  • Essential amino acids: not synthesized by the body and must be obtained from the diet
  • Branched-chain amino acids (BCAAs) are essential and crucial in maintaining muscle tissue.
  • Limiting amino acids are found in the smallest quantities in some foods (e.g., lysine and threonine in cereals, methionine and cysteine in legumes)

Conditionally Essential Amino Acids

  • Normally synthesized by the body
  • May become essential during certain physiological conditions

Physiological Functions of Proteins

  • Tissue growth and maintenance
  • Synthesis of other proteins
  • Regulation of bodily processes and immune function
  • Provide energy

Protein Metabolism

  • Primary function: supplies material for growth and maintenance of body tissues
  • Anabolism: Production of new cellular material
  • Catabolism: Breaking down or destruction of body tissues
  • Anabolism and catabolism are continuous and simultaneous processes

Dietary Protein and Nitrogen Balance

  • Dietary proteins provide approximately 1 gram of nitrogen for every 6.25 grams of protein consumed
  • Nitrogen is excreted through urine, feces, and sweat
  • Nitrogen equilibrium: intake equals loss
  • Negative nitrogen balance: intake is less than loss (e.g., burn, hyperthyroidism, fasting, fever)
  • Positive nitrogen balance: intake is greater than loss (e.g., pregnancy, growth, tissue repair)

Enzymes

  • Proteins that catalyze biochemical reactions in all living cells
  • Crucial for digestion and metabolism

Hormones

  • Proteins that act as chemical messengers in the body, regulating physiological processes
  • Thyroid hormones regulate metabolic rate and cellular development
  • Insulin and glucagon maintain blood glucose concentration

Buffering

  • Proteins act as buffers, keeping fluids and tissues at a constant pH
  • Amino acids contribute to the buffering system by releasing or accepting hydrogen ions

Fluid Balance

  • Proteins maintain proper fluid balance by influencing osmotic pressure
  • Proteins in blood vessels pull fluid back into capillaries, preventing fluid buildup (edema) in tissues

Immune Response

  • Proteins are a component in cells used during an immune response
  • The body synthesizes antibodies to target and neutralize harmful substances
  • Each antibody is tailored to a specific antigen

Protein as an Energy Source

  • Proteins can be used as an energy source when fats and carbohydrates are not sufficient
  • This process leads to depletion of lean body tissue

Protein Digestion

  • Stomach: Hydrochloric acid denatures proteins and activates pepsin to break peptide bonds
  • Small Intestine: Partially digested proteins trigger the release of regulatory peptides that signal the pancreas to release digestive proenzymes (inactive enzymes)
  • Small Intestine (cont.): Activated enzymes break down polypeptides into amino acids which are absorbed by the small intestine.

Post-Digestion Actions

  • Intestinal cells utilize some absorbed peptides and amino acids for energy and synthesis of other compounds
  • Remaining amino acids are transported into the liver
  • The liver monitors the absorbed amino acids and regulates their metabolism

Amino Acid Catabolism

  • Deamination: Process of removing nitrogen from a substance to convert ammonia to urea for excretion by the kidneys
  • Transamination: Transfer of nitrogen from one chemical group to another without ammonia formation.

Protein Turnover

  • Continuous synthesis and degradation of proteins within the body
  • New amino acids join with existing amino acids to form a readily available amino acid pool

Protein Quality

  • Assesses protein composition and digestibility
  • Digestibility depends on the protein source and other foods ingested
  • Protein digestibility-corrected amino acid score (PDCAA) quantifies protein quality based on composition and digestibility

Protein Sources

  • Two main categories: complete (high-quality) and incomplete (low-quality)
  • Complete proteins contain all essential amino acids in correct amounts (e.g., animal proteins, soy)
  • Incomplete proteins lack one or more essential amino acids (e.g., most plant proteins)
  • Complementary proteins are different food sources that, when combined, provide all essential amino acids
  • Protein RDA for adults aged 19-70: approximately 0.8 g/kg/day
  • Infants, children, and pregnant women have slightly higher protein needs.
  • Recommended protein intake varies by age, weight, and other factors

Inborn Errors of Metabolism

  • Inherited defects in substrate metabolism
  • Examples include phenylketonuria (PKU), which results in harmful phenylalanine buildup and requires a diet low in phenylalanine

Malnutrition

  • Insufficient intake of nitrogen-containing foods resulting in malnutrition
  • Two main forms:
    • Kwashiorkor: Adequate energy intake but insufficient protein intake
    • Marasmus: Inadequate consumption of energy resulting in compromised protein status and significant weight loss
    • Treatment involves identifying the cause and ensuring adequate intake of both protein and energy

Additional Note

  • A YouTube link is provided for further information about protein roles.

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Test your knowledge on protein structure, composition, and the physiological functions of proteins. This quiz covers amino acids, their classifications, and dietary recommendations for protein intake. Additionally, challenge your understanding of protein metabolism and associated disorders.

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