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Questions and Answers
What are the building blocks of proteins?
What are the building blocks of proteins?
Amino acids
What does a side chain dictate?
What does a side chain dictate?
The function of that amino acid
What type of bond links amino acids together?
What type of bond links amino acids together?
Peptide bonds
What is the term for 10 or more amino acids bonded together?
What is the term for 10 or more amino acids bonded together?
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Nonessential amino acids are required in the diet.
Nonessential amino acids are required in the diet.
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Essential amino acids are produced by the body.
Essential amino acids are produced by the body.
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Which of the following are examples of branched chain amino acids involved in maintaining muscle tissue? (Select all that apply)
Which of the following are examples of branched chain amino acids involved in maintaining muscle tissue? (Select all that apply)
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What are limiting amino acids, and where are they typically found?
What are limiting amino acids, and where are they typically found?
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What are conditionally essential amino acids, and why are they important?
What are conditionally essential amino acids, and why are they important?
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What are some of the physiologic functions of proteins? (Select all that apply)
What are some of the physiologic functions of proteins? (Select all that apply)
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What is the primary function of protein in the body?
What is the primary function of protein in the body?
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Describe the difference between anabolism and catabolism.
Describe the difference between anabolism and catabolism.
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How much nitrogen is provided by 6.25 grams of protein consumed?
How much nitrogen is provided by 6.25 grams of protein consumed?
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What is nitrogen balance, and what are the different types?
What is nitrogen balance, and what are the different types?
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What is the role of proteins in enzyme production?
What is the role of proteins in enzyme production?
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Enzymes are catalysts for biochemical reactions.
Enzymes are catalysts for biochemical reactions.
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Enzymes are specific to their substrates and reactions.
Enzymes are specific to their substrates and reactions.
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What is the role of proteins in hormone production?
What is the role of proteins in hormone production?
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Give an example of how proteins are involved in hormone regulation.
Give an example of how proteins are involved in hormone regulation.
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What is a buffer, and how do proteins act as buffers?
What is a buffer, and how do proteins act as buffers?
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What is oncotic pressure, and how does it affect fluid balance?
What is oncotic pressure, and how does it affect fluid balance?
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What is edema?
What is edema?
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Proteins are involved in the immune response by producing antibodies to attack antigens.
Proteins are involved in the immune response by producing antibodies to attack antigens.
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Each antibody is specific to a particular antigen.
Each antibody is specific to a particular antigen.
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The body keeps a record of the characteristics of each antibody manufactured, allowing it to produce the same antibodies more quickly in the future.
The body keeps a record of the characteristics of each antibody manufactured, allowing it to produce the same antibodies more quickly in the future.
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When do proteins provide a source of energy?
When do proteins provide a source of energy?
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Depletion of lean body tissue can occur when the body breaks down muscle for energy.
Depletion of lean body tissue can occur when the body breaks down muscle for energy.
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What is the importance of adequate intake of all macronutrients?
What is the importance of adequate intake of all macronutrients?
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What happens to proteins in the stomach during digestion?
What happens to proteins in the stomach during digestion?
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What is the role of the enzyme pepsin in protein digestion?
What is the role of the enzyme pepsin in protein digestion?
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Where do polypeptides and free amino acids go after being partially digested in the stomach?
Where do polypeptides and free amino acids go after being partially digested in the stomach?
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How do partially digested proteins elicit the release of regulatory peptides?
How do partially digested proteins elicit the release of regulatory peptides?
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What is the function of proenzymes in protein digestion?
What is the function of proenzymes in protein digestion?
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What happens after intestinal degradation of proteins?
What happens after intestinal degradation of proteins?
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What is the role of the liver in amino acid metabolism?
What is the role of the liver in amino acid metabolism?
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Deamination is the process by which nitrogen is removed from a substance.
Deamination is the process by which nitrogen is removed from a substance.
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The body converts ammonia to urea for excretion by the kidneys.
The body converts ammonia to urea for excretion by the kidneys.
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What is the function of the carbon skeleton remaining after deamination?
What is the function of the carbon skeleton remaining after deamination?
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What is transamination?
What is transamination?
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What is protein turnover?
What is protein turnover?
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Describe the formation of an amino acid pool during protein turnover.
Describe the formation of an amino acid pool during protein turnover.
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What is the significance of a stable amino acid pool in protein turnover?
What is the significance of a stable amino acid pool in protein turnover?
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What factors are assessed in protein quality?
What factors are assessed in protein quality?
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What is the Protein Digestibility Corrected Amino Acid Score (PDCAA)?
What is the Protein Digestibility Corrected Amino Acid Score (PDCAA)?
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What is the difference between complete and incomplete proteins?
What is the difference between complete and incomplete proteins?
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Give examples of sources for complete and incomplete proteins.
Give examples of sources for complete and incomplete proteins.
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Describe complementary proteins.
Describe complementary proteins.
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What is the RDA for protein in adults aged 19-70?
What is the RDA for protein in adults aged 19-70?
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Infants, children, and pregnant women require slightly higher protein intakes than adults.
Infants, children, and pregnant women require slightly higher protein intakes than adults.
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What is an inborn error of metabolism, and give an example.
What is an inborn error of metabolism, and give an example.
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Describe the dietary implications for individuals with phenylketonuria (PKU)?
Describe the dietary implications for individuals with phenylketonuria (PKU)?
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What is the impact of stress induced by critical injury on nitrogen balance?
What is the impact of stress induced by critical injury on nitrogen balance?
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Which of the following conditions necessitate elevated protein intake? (Select all that apply)
Which of the following conditions necessitate elevated protein intake? (Select all that apply)
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Higher protein intake is needed during recovery from severe burns.
Higher protein intake is needed during recovery from severe burns.
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Why does certain types of kidney or liver failure necessitate reduced protein intake?
Why does certain types of kidney or liver failure necessitate reduced protein intake?
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Describe protein malnutrition and what it leads to.
Describe protein malnutrition and what it leads to.
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What are the characteristics of Kwashiorkor?
What are the characteristics of Kwashiorkor?
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What are the characteristics of marasmus?
What are the characteristics of marasmus?
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What are the general steps involved in treating malnutrition?
What are the general steps involved in treating malnutrition?
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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
Recommended Dietary Allowances (RDAs)
- 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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Description
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.