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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

Diagnosis of acute viral hepatitis may be estimated by determination of activity of which enzyme?

  • Kreatine kinase (MB isoform)
  • Gamma-glutamyltranspeptidase (correct)
  • Lactate dehydrogenase (isoforms 4, 5)
  • Lactate dehydrogenase (isoforms 1, 2)
  • Diagnosis of acute pancreatitis may be estimated by determination of activity of which enzyme?

  • Amylase (correct)
  • Lactate dehydrogenase (isoforms 1, 2)
  • Alanine aminotransferase
  • Lipase
  • Aerobic dehydrogenation is a variant of oxidation reaction, which enzyme catalyzes this reaction?

  • Cytochrome oxidase (correct)
  • Monoaminooxidase
  • Cytochrome P450
  • Phenylalanine monooxygenase
  • Which type of oxidation reactions involve removal of electrons?

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

    What significant role do monooxygenases play?

    <p>Xenobiotics detoxication</p> Signup and view all the answers

    Main function of glycosphingolipids is:

    <p>Components of cellular membranes</p> Signup and view all the answers

    Main function of glycerophospholipids is:

    <p>Components of cellular membranes</p> Signup and view all the answers

    What is true as a description of chylomicrons?

    <p>They have the largest diameter among all lipoproteins</p> Signup and view all the answers

    Transport of exogenous lipids from intestine to tissues is provided by…

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

    Ketone bodies can be synthesized in…

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

    Normal serum concentration range of ketone bodies is…

    <p>0-30 mg/l</p> Signup and view all the answers

    Normal serum concentration range of cholesterol is…

    <p>3.5-5.2 mmol/l</p> Signup and view all the answers

    Normal serum concentration range of free fatty acids is…

    <p>0.48-0.68 mmol/l</p> Signup and view all the answers

    Normal serum concentration range of total lipids is…

    <p>4-8 g/l</p> Signup and view all the answers

    The source of carbon atoms for fatty acids synthesis is…

    <p>Acetyl-CoA</p> Signup and view all the answers

    Choose the metabolic pathway in which amino acids cannot be used:

    <p>Protein synthesis</p> Signup and view all the answers

    Choose the urea cycle reaction which is catalyzed by a mitochondrial enzyme:

    <p>Synthesis of Krebs cycle intermediate</p> Signup and view all the answers

    Choose the substance that is regenerated in each round of transdeamination reactions:

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

    Methylation (transmethylation) reactions are used for:

    <p>Urea synthesis</p> Signup and view all the answers

    Deficiency of folic acid and cobalamin may cause:

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

    Ammonia is toxic due to?

    <p>Decrease of glutamate concentration in mitochondria</p> Signup and view all the answers

    Accumulation of arginine in blood is a result of a genetic defect in synthesis of:

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

    Alkaptonuria is a result of genetic defect in:

    <p>Homogentisate oxidase</p> Signup and view all the answers

    Accumulation of argininosuccinate in blood is a result of a genetic defect in synthesis of:

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

    Classic variant of phenylketonuria is a result of genetic defect in:

    <p>Phenylalanine hydroxylase</p> Signup and view all the answers

    Genetic disorder (metabolic disease) hyperammonemia type I is a result of a defect in the:

    <p>Carbamoylphosphate synthase I</p> Signup and view all the answers

    Functions of serotonin include:

    <p>Neurotransmitter in sympathetic nervous system</p> Signup and view all the answers

    Biogenic amines are inactivated by:

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

    Functions of adrenaline include:

    <p>Neurotransmitter in CNS</p> Signup and view all the answers

    Regeneration of methionine from homocysteine requires:

    <p>N5,N10-methylene-H4-folate</p> Signup and view all the answers

    Functions of histamine include:

    <p>Inducer of gastric juice secretion</p> Signup and view all the answers

    The bases which can be found in purine nucleotides are:

    <p>Adenine and guanine</p> Signup and view all the answers

    The bases which can be found in pyrimidine nucleotides are:

    <p>Thymine and cytosine</p> Signup and view all the answers

    Monomers in the structure of RNA are:

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

    Monomers in the structure of DNA are:

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

    Nucleotides which can be used in DNA biosynthesis are:

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

    Nucleotides which can be used in RNA biosynthesis are:

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

    The bond between nucleotides in the primary structure of nucleic acid is...

    <p>5',3'-phosphodiester bond</p> Signup and view all the answers

    The complementary pair of bases in the secondary structure of DNA is...

    <p>Guanine-Thymine</p> Signup and view all the answers

    The secondary structure of DNA is stabilized by...

    <p>Hydrogen bonds</p> Signup and view all the answers

    Choose the tetrapeptide which has TWO amino acid residues with hydrophobic side chains:

    <p>Trp-Ile-Cys-Val</p> Signup and view all the answers

    Choose the tetrapeptide which has THREE amino acid residues with hydrophilic side chains:

    <p>Val-Cys-Met-Ser</p> Signup and view all the answers

    Choose the tetrapeptide which has N-terminal amino acid residue with hydrophobic side chain:

    <p>Phe-Tyr-Lys-Val</p> Signup and view all the answers

    Choose the tetrapeptide which has TWO amino acid residues with hydrophilic side chains:

    <p>Asn-Val-Val-Met</p> Signup and view all the answers

    Choose the tetrapeptide which has C-terminal amino acid residue with hydrophilic side chain:

    <p>Val-Ser-Tre-Met</p> Signup and view all the answers

    Choose the tetrapeptide which has THREE amino acid residues with hydrophilic side chains:

    <p>Ser-Gly-Trp-Pro</p> Signup and view all the answers

    The primary structure in ALL proteins is stabilized with…

    <p>Peptide bonds</p> Signup and view all the answers

    The secondary structure of proteins is stabilized ONLY with…

    <p>Hydrogen bonds</p> Signup and view all the answers

    The tertiary structure of proteins is stabilized with…

    <p>Covalent or/and noncovalent bonds</p> Signup and view all the answers

    The quaternary structure of proteins is stabilized mainly with…

    <p>Noncovalent bonds and hydrophobic interactions</p> Signup and view all the answers

    Indicate a function which is NOT performed by proteins in humans:

    <p>Storing of genetic information</p> Signup and view all the answers

    How is glucagon inactivated?

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

    Choose a pair of hormones regulating exchange of water and minerals.

    <p>Aldosterone and vasopressin</p> Signup and view all the answers

    Choose a pair of hormones regulating reproductive functions.

    <p>Testosterone and estradiol</p> Signup and view all the answers

    Choose a pair of hormones regulating exchange of calcium and phosphates.

    <p>Calcitriol and calcitonin</p> Signup and view all the answers

    All effects listed below are shared by glucagon and cortisol except...

    <p>Stimulation of lipogenesis in the adipose tissue</p> Signup and view all the answers

    Choose appropriate effects of cortisol.

    <p>Stimulate lipogenesis in the adipose tissue</p> Signup and view all the answers

    Choose appropriate effects of insulin action on cells.

    <p>Stimulate lipogenesis in the adipose tissue</p> Signup and view all the answers

    Choose appropriate effects of adrenalin.

    <p>Stimulate glycogenolysis in muscles</p> Signup and view all the answers

    Choose appropriate effects of glucagon.

    <p>Increase glycogen breakdown in the liver</p> Signup and view all the answers

    Choose appropriate effects of insulin action on cells.

    <p>Increase glycogen synthesis in the liver</p> Signup and view all the answers

    All metabolic pathways listed below do not work in erythrocytes except:

    <p>Oxidative phosphorylation</p> Signup and view all the answers

    Choose substance which decreases Hb affinity to oxygen.

    <p>2,3-bisphosphoglycerate</p> Signup and view all the answers

    Choose a variant of Hb which cannot transport oxygen in blood.

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

    ATP in red blood cells is used mainly for...

    <p>Active transport</p> Signup and view all the answers

    Increase of affinity and rate of O2 binding to Hb is a result of...

    <p>Positive cooperative effect</p> Signup and view all the answers

    Study Notes

    Protein Structure, Properties, and Functions

    • A protein's primary structure is stabilized by peptide bonds.
    • The secondary structure of proteins is stabilized by hydrogen bonds.
    • The tertiary structure of proteins is stabilized by covalent and noncovalent bonds.
    • The quaternary structure of proteins is stabilized by noncovalent bonds and hydrophobic interactions.
    • Functions of proteins in humans:
      • Transport of hormones in blood
      • Muscle contraction
      • Storage of genetic information
      • Catalysis of reactions
    • Globulins are poorly dissolved in pure water, but their solubility can be increased by adding small amounts of NaCl.
    • Protein-ligand interactions:
      • Examples: antigen-antibody, hormone-receptor, and protein-heavy metal ion interactions
      • Binding of ligand is highly specific and necessary for performing specific biological functions

    Enzymes and Cofactors

    • Cofactors:
      • Vitamin B5 (nicotinic acid): part of coenzyme NAD
      • Vitamin B2 (riboflavin): part of coenzyme FAD
      • Vitamin B1 (thiamin): part of coenzyme TPP
      • Vitamin B6: part of coenzyme pyridoxal phosphate
      • Vitamin B9 (folic acid): part of coenzyme THF
    • Enzyme cofactor functions:
      • FAD: intermediate carrier of hydrogen atoms
      • HS-CoA: intermediate carrier of acyl groups
      • NAD: intermediate carrier of hydrogen atoms
      • THF: intermediate carrier of one-carbon groups
      • Pyridoxal phosphate: intermediate carrier of amino groups
    • Enzyme classification:
      • Transferases: catalyze the transfer of functional groups
      • Ligases: catalyze the formation of covalent bonds
      • Lyases: catalyze the cleavage of various chemical bonds
      • Oxidoreductases: catalyze oxidation and reduction reactions

    Energy Exchange

    • Aerobic dehydrogenation: catalyzed by cytochrome oxidase
    • Anaerobic dehydrogenation: catalyzed by succinate dehydrogenase
    • Oxidation by removal of electrons: catalyzed by cytochrome a
    • Dehydrogenation: a type of oxidation reaction in which electrons are removed from the substrate
    • Monooxygenases: play a significant role in xenobiotics detoxication and the generation of reductive potentials
    • Caloric coefficients:
      • Carbohydrates: 4.1 kcal/g
      • Proteins: 4.1 kcal/g
      • Lipids: 9.3 kcal/g
    • Daily requirements for food components (according to the WHO recommendations):
      • Lipids: 1-2 g/kg body weight
      • Proteins: 1-2 g/kg body weight
      • Carbohydrates: 2-3 g/kg body weight
    • Krebs cycle enzymes:
      • Citrate synthase
      • Aconitase
      • Isocitrate dehydrogenase
      • α-ketoglutarate dehydrogenase complex
      • Succinyl-CoA-synthase
      • Succinate dehydrogenase
      • Fumarase
      • Malate dehydrogenase
    • Inhibitors of the respiratory chain:
      • Complex I: rotenon
      • Complex II: carboxin
      • Complex III: antimycin
      • Complex IV: carbon monoxide
    • Uncoupling effect on oxidative phosphorylation:
      • Caused by Dinitrophenol, Acetylsalicylic acid, and other substances

    Carbohydrates

    • Classification of carbohydrates:
      • Monosaccharids: e.g., galactose
      • Disaccharids: e.g., sucrose
      • Homopolysaccharids: e.g., glycogen
      • Heteropolysaccharids: e.g., hialuronic acid
    • Metabolic pathways:
      • Glycolysis: anaerobic oxidation of glucose
      • Gluconeogenesis: synthesis of glucose from non-carbohydrate substances
      • Pentose phosphate pathway: generation of NADPH+H+
      • Glycogenesis: synthesis of glycogen from glucose
      • Glucogenolysis: breakdown of glycogen to glucose### Carbohydrate Metabolism
    • Digestion of glycogen and starch in the oral cavity is catalyzed by amylase.
    • Digestion of disaccharides in the small intestine is catalyzed by sucrase, lactase, and maltase.
    • All sugars can be absorbed in the intestinal wall, except lactose, ribose, and galactose.
    • Products of food carbohydrates digestion in the GIT can be absorbed by active transport, facilitated diffusion, and simple diffusion.
    • Hormones that have a hyperglycemic effect are glucagon, adrenalin, and cortisol, whereas insulin decreases blood glucose concentration.
    • A patient has hyperglycemia if the concentration of glucose in blood is above 6.2 mmol/l, and hypoglycemia if it's below 3.6 mmol/l.
    • Normal range of glucose concentration in blood in adults is 2.2-4.4 mmol/l.
    • Physiologic hypoglycemia can be found in healthy persons in cases of starvation, and physiologic hyperglycemia in cases of overconsumption of food carbohydrates, long-term hard physical activity, or emotional stress.

    Lipids

    • Saturated fatty acids include palmitic acid, and polyunsaturated fatty acids include linoleic acid.
    • Monounsaturated fatty acids include oleic acid.
    • Eicosanoids are products of metabolism of the fatty acid arachidonic acid.
    • The main function of triacylglycerols is energy storage.
    • Cholesterol plays several physiological functions, including being a precursor for steroid hormones, and a component of cell membranes.
    • The main function of eicosanoids is to act as regulative molecules of the paracrine system.
    • Fatty acids may perform functions such as being structural components of cell membranes, and sources of energy.
    • The main function of glycosphingolipids is to act as components of cellular membranes.
    • The main function of glycerophospholipids is to act as components of cellular membranes.
    • Ketone bodies can be synthesized in hepatocytes.
    • Normal serum concentration range of ketone bodies is 0-30 mg/l.

    Proteins and Amino Acids Exchange

    • Essential amino acids include phenylalanine, methionine, tryptophan, and cysteine.
    • Nitrogen equilibrium may be observed in healthy adults, and negative nitrogen balance may be observed in starvation state.
    • Positive nitrogen balance may be observed in healthy children, and in cases of protein synthesis.
    • Chymotrypsinogen is activated by trypsin.
    • Amino acids can be used in protein synthesis, gluconeogenesis, and oxidative breakdown.
    • Transamination is a process of transfer of an amino group from an amino acid to a keto acid.
    • Transdeamination includes two reactions: transamination with oxaloacetate, and oxidative deamination of Asp.
    • Enzymes that catalyze transdeamination reactions have cofactors such as pyridoxalphosphate and NAD+.
    • Decarboxylation of amino acids and their metabolites needs a cofactor such as pyridoxalphosphate.
    • The amino acid pool includes approximately 30 grams of free amino acids.
    • Amino acids cannot be used in glycolysis.
    • Choose the substance which is regenerated in each round of transdeamination reactions: α-ketoglutarate.

    Nucleic Acids and Nucleotides

    • The bases that can be found in purine nucleotides are adenine and guanine.
    • The bases that can be found in pyrimidine nucleotides are thymin and cytosin.
    • Monomers in the structure of RNA are AMP, GMP, CMP, and UMP.
    • Monomers in the structure of DNA are dAMP, dGMP, dCMP, and dTMP.### DNA Biosynthesis
    • Nucleotides used in DNA biosynthesis: dATP, dGTP, dCTP, dTTP
    • Bond between nucleotides in primary structure of nucleic acid: 3',5'-phosphodiester bond
    • Complementary pair of bases in secondary structure of DNA: Adenine-Thymine, Guanine-Cytosine
    • Secondary structure of DNA is stabilized by: hydrogen bonds

    DNA Folding

    • Sequence of DNA folding events: Nucleosomes → 30-nm fibrils → Loops → Chromosomes
    • Length of separate DNA molecule: several centimeters
    • Enzyme that unwinds double helix during DNA replication: Helicase
    • Enzyme that prevents supercoil formation during DNA replication: Topoisomerase
    • Enzyme that synthesizes oligoribonucleotide during DNA replication: Primase

    Regulation of Metabolism

    • Hormone synthesis locations:
      • Glucagon: Pancreatic gland
      • Thyroxine: Thyroid gland
      • Adrenalin: Medulla of suprarenal glands
      • Somatotropin: Pituitary gland
    • Hormone types:
      • Peptide hormones: Glucagon, growth hormone, insulin
      • Derivatives of amino acids: Adrenalin, thyroxine, T3, T4
      • Steroid hormones: Aldosteron, cortisol, calcitriol, testosteron
    • Hormone receptors:
      • Insulin, growth hormone, glucagon: outer cell membrane
      • Thyroxine, aldosteron: nucleus
      • Adrenalin: outer cell membrane
    • Hormone inactivation:
      • Insulin: Oxidative deamination and conjugation
      • Adrenalin: Oxidative deamination and methylation
      • Glucagon: Proteolysis

    Biochemistry of Blood, Liver, Kidney, and Connective Tissue

    • Metabolic pathways in erythrocytes:
      • Pentose phosphate pathway
      • Anaerobic glycolysis
      • Glutathione regeneration
    • Substances that decrease Hb affinity to oxygen: 2,3-bisphosphoglycerate
    • Variants of Hb: OxyHb, MetHb, HbF, CarboxyHb
    • ATP usage in red blood cells: For active transport
    • Pathologic variant of Hb: HbS
    • Hyperazotemia: Urea nitrogen percentage more than 30%
    • Glucokinase kinetic properties: High value of Km, not inhibited by glucose-6-phosphate
    • Lipoproteins produced by hepatocytes: VLDL and HDL
    • Bilirubin detoxication in the liver: Glucuronidation

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    Prepare for your examination test with these questions on protein structure, properties, and functions. Identify tetrapeptides with hydrophobic and hydrophilic side chains.

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