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Questions and Answers
What is the function of enzymes in the context of proteins?
What is the function of enzymes in the context of proteins?
Which of the following is NOT a factor that can denature a protein?
Which of the following is NOT a factor that can denature a protein?
What is the significance of the isoelectric point (pI) of a protein?
What is the significance of the isoelectric point (pI) of a protein?
Which protein structure level is primarily responsible for the functional properties of a protein?
Which protein structure level is primarily responsible for the functional properties of a protein?
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What is the defining characteristic that distinguishes proteins from carbohydrates and lipids?
What is the defining characteristic that distinguishes proteins from carbohydrates and lipids?
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Which of the following proteins is an example of a protein with a quaternary structure?
Which of the following proteins is an example of a protein with a quaternary structure?
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How is the synthesis rate of a protein determined?
How is the synthesis rate of a protein determined?
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What is the primary role of immunoglobulins in the body?
What is the primary role of immunoglobulins in the body?
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Which of the following properties is NOT typically used to describe a protein?
Which of the following properties is NOT typically used to describe a protein?
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Which of the following conditions is associated with decreased levels of alpha 1-acid glycoprotein?
Which of the following conditions is associated with decreased levels of alpha 1-acid glycoprotein?
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What is the primary function of alpha 1-antitrypsin?
What is the primary function of alpha 1-antitrypsin?
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Which of the following is NOT a characteristic of Alpha 1-Fetoprotein (AFP)?
Which of the following is NOT a characteristic of Alpha 1-Fetoprotein (AFP)?
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What is the primary function of Alpha 1-Acid Glycoprotein?
What is the primary function of Alpha 1-Acid Glycoprotein?
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Which of the following conditions is associated with high levels of alpha 1-acid glycoprotein?
Which of the following conditions is associated with high levels of alpha 1-acid glycoprotein?
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Which of the following is true about alpha 1-antitrypsin?
Which of the following is true about alpha 1-antitrypsin?
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Which of the following plasma proteins is considered an acute-phase reactant?
Which of the following plasma proteins is considered an acute-phase reactant?
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Which of the following plasma proteins is specifically involved in fetal development?
Which of the following plasma proteins is specifically involved in fetal development?
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What is the main function of alpha 1-antichymotrypsin?
What is the main function of alpha 1-antichymotrypsin?
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What is the main function of IgM in the immune response?
What is the main function of IgM in the immune response?
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Which of the following immunoglobulins can cross the placenta?
Which of the following immunoglobulins can cross the placenta?
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What is a significant use of cardiac troponin (cTn) in clinical diagnosis?
What is a significant use of cardiac troponin (cTn) in clinical diagnosis?
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Which plasma protein is associated with congestive heart failure and is released by the heart?
Which plasma protein is associated with congestive heart failure and is released by the heart?
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What condition is indicated by low levels of protein in the blood, known as hypoproteinemia?
What condition is indicated by low levels of protein in the blood, known as hypoproteinemia?
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What substance must be restricted in the diet of individuals with Homocystinuria?
What substance must be restricted in the diet of individuals with Homocystinuria?
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Which aminoacidopathy is characterized by a burnt sugar odor of urine?
Which aminoacidopathy is characterized by a burnt sugar odor of urine?
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What is the main treatment for Tyrosinemia type I?
What is the main treatment for Tyrosinemia type I?
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Which enzyme is deficient in individuals with Alkaptonuria?
Which enzyme is deficient in individuals with Alkaptonuria?
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What is a common diagnostic test for Cystinuria?
What is a common diagnostic test for Cystinuria?
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What structural level of protein is formed by a sequence of amino acids linked together?
What structural level of protein is formed by a sequence of amino acids linked together?
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Which aminoacidopathy is linked to kidney stones due to a defect in amino acid transport?
Which aminoacidopathy is linked to kidney stones due to a defect in amino acid transport?
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What is a characteristic of Beta 2-Microglobulin?
What is a characteristic of Beta 2-Microglobulin?
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In which condition would you expect elevated levels of C-Reactive Protein (CRP)?
In which condition would you expect elevated levels of C-Reactive Protein (CRP)?
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What is the primary role of Complement proteins?
What is the primary role of Complement proteins?
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Which globulin is classified as an acute-phase reactant?
Which globulin is classified as an acute-phase reactant?
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What could cause decreased levels of Fibrinogen?
What could cause decreased levels of Fibrinogen?
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Which type of immunoglobulin is primarily increased in liver disease?
Which type of immunoglobulin is primarily increased in liver disease?
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What is the significance of elevated levels of C-Reactive Protein (CRP)?
What is the significance of elevated levels of C-Reactive Protein (CRP)?
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What happens to Beta 2-Microglobulin levels in cases of impaired kidney clearance?
What happens to Beta 2-Microglobulin levels in cases of impaired kidney clearance?
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What is the primary function of Fibrinogen in plasma?
What is the primary function of Fibrinogen in plasma?
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In what condition might you see increased levels of Complement proteins?
In what condition might you see increased levels of Complement proteins?
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Study Notes
Amino Acids and Proteins
- Proteins are the building blocks of life, supporting various biological activities like growth, repair, and maintenance.
- Twenty amino acids are essential for these bodily functions.
- Half of the amino acids must be acquired through diet.
Classification of Amino Acids
- Amino acids have both an amino group and a carboxylic acid functional group.
- Alpha amino acids feature an amino group directly bonded to the alpha-carbon.
- Each alpha amino acid has a unique R group attached to the alpha carbon.
Peptide Bonds
- A peptide bond is an amide bond forming between a carboxyl group of one amino acid and an amino group of another amino acid.
Essential and Nonessential Amino Acids
- Essential amino acids are obtained from diet.
- Nonessential amino acids can be produced by the body.
- Essential amino acids include: Valine, Leucine, Isoleucine, Methionine, Tryptophan, Phenylalanine, Threonine, Lysine, and Histidine.
- Many others are categorized as nonessential.
Amino Acid Synthesis
- Proteolytic enzymes like Pepsin and Trypsin break down dietary proteins into amino acids.
- These enzymes remove amino groups from amino acids.
- Deamination breaks down amino acids, and transamination transfers amino acids.
Aminoacidopathies
- Aminoacidopathies are inherited metabolic disorders.
- These disorders are caused by enzyme deficiencies leading to amino acid build-up.
Types of Aminoacidopathies
- Phenylketonuria (PKU): a deficiency in phenylalanine hydroxylase resulting in phenylalanine buildup and mental retardation. Common symptoms include: musty urine odor, phenylalanine in excess can cause mental retardation.
- Tyrosinemia type I is the most severe type of tyrosinemia involving tyrosine, with high excretion of tyrosine and tyrosine catabolites in the urine. Typical symptoms of tyrosinemia include kidney and liver failure and cirrhosis. Treatment includes low protein diet and drug nitisinone.
- Alkaptonuria (lack of homogentisate oxidase) causes excess of homogentistate acid making urine to turn black when left at room temperature.. Symptoms can include arthritic symptoms later in life and development of arthritis; Treatment is with Vitamin C.
- Maple Syrup Urine Disease (MSUD): deficiency in alpha-ketoacid decarboxylase, causing a high level of leucine, isoleucine, and valine in the body in babies, and characteristic maple syrup odor of urine, skin, and breath.
- Homocystinuria: lack of cystathionine beta-synthase, preventing the breakdown of methionine. Symptoms can include muscle weakness, CNS problems, bone abnormalities, and thrombosis.
- Cystinuria: defective amino acid transport system in the renal tubules preventing reabsorption of cysteine. Typical symptoms include kidney stones. Treatment includes high fluid intake to prevent cystine stone formation.
Protein Structures
- Primary Structure: linear sequence of amino acids linked together from the N-terminus to the C-terminus (e.g., hemoglobin).
- Secondary Structure: repeating structures stabilized by hydrogen bonds (e.g., alpha-helix, beta-pleated sheets).
- Tertiary Structure: overall shape of a protein formed by interactions between side chains which can bond and form functional properties.
- Quaternary Structure: interaction of multiple protein molecules to form a larger functional protein (e.g., hemoglobin).
Denaturation of Proteins
- Denaturation is the disruption of protein structure, causing loss of function. This occurs when certain factors interfere with the structure like Heat, Hydrolysis, strong acid (pH), strong alkali (pH), enzymatic action, urea exposure or other substance, ultraviolet exposure, and heavy metals and solvents.
Proteins Characteristics
- Proteins are described by their content like nitrogen content (approximately 16%.), charge (isoelectric point), and solubility (hydrophilic).
- Proteins contain carbon, hydrogen, oxygen, sulfur, and nitrogen unlike carbon/lipids that don't contain nitrogen.
Functions ofProteins
- Enzymes: catalyze biochemical reactions.
- Hormone receptors: bind hormones to trigger cellular responses.
- Transporters: carry molecules across membranes.
- Immunoglobulins: protect against foreign invaders.
- Structural proteins: provide support and shape.
- Storage proteins: store amino acids or other molecules.
- Energy source: provide energy when other sources are depleted.
- Osmotic force: helps maintain fluid balance.
- Tissue nutrition: provide nutrients for tissues.
Two Major Classifications of Proteins
- Simple proteins: composed solely of amino acids.
- Conjugated proteins: contain both an amino acid component and a non-protein component (e.g., glycoproteins, lipoproteins).
Plasma Proteins
- Plasma proteins are proteins in the blood; They include albumin, globulins, and other important proteins like fibrinogen, transferrin, and immunoglobulins.
Plasma Protein Methods
- Electrophoresis is a method to separate proteins based on charges and sizes in the blood.
- Dye-binding is a method for measuring albumin by using dyes that bind only to albumin.
Proteins in Other Body Fluids
- Urinary protein: qualitative (reagent test strips) and quantitative (24-hour urine specimen).
- Cerebrospinal fluid (CSF) protein: measures protein in CSF (to determine if damage to blood barrier; during disease or trauma).
Other Plasma Proteins
- Myoglobin, Cardiac Troponin, BNP, Fibronectin,
- Myoglobin: single-chain globulin (153 amino acids), contains heme group, cardiac biomarker, toxic to kidneys.
- Cardiac Troponin: represents a complex of regulatory proteins; important for diagnosing acute coronary syndrome.
- BNP: released by heart in response to congestive heart failure, indicating heart muscle dysfunction.
- Fibronectin: amniotic sac protein; detects pre-term labor through amniotic fluid, etc.
Total Protein Abnormalities
- Hypoproteinemia (low total protein): causes include excessive protein loss, poor protein absorption, or decreased protein intake.
- Hyperproteinemia (high total protein) causes include dehydration and other conditions.
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Description
Test your knowledge on amino acids and proteins, essential for life. This quiz covers topics like the classification of amino acids, peptide bonds, and the differences between essential and nonessential amino acids. Understand the critical functions of these biological molecules in nutrition and metabolism.
