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Questions and Answers
Which of following bonds don't participate in formation of tertiary structure of proteins?
Which of following bonds don't participate in formation of tertiary structure of proteins?
- Hydrophobic interactions
- Hydrogen bond
- Disulfide bond
- Ionic bond
- Coordination bond (correct)
Casein concerns to a class of:
Casein concerns to a class of:
- Phosphoproteins (correct)
- Lipoproteins
- Glycoproteins
- Chromoproteins
- Metalloproteins
The amino acid which is not meeting in structure of a molecule of proteins:
The amino acid which is not meeting in structure of a molecule of proteins:
- Proline
- Gytamic acid
- Beta-alanine (correct)
- Lysine
- Phenylalanine
Show the iminoacid:
Show the iminoacid:
What amino acid contains sulfur:
What amino acid contains sulfur:
Quaternary structure of a molecule of hemoglobin is described by the formula:
Quaternary structure of a molecule of hemoglobin is described by the formula:
Basic simple proteins of nucleoproteins of humans are:
Basic simple proteins of nucleoproteins of humans are:
Function of nucleic acids is:
Function of nucleic acids is:
The proteins which are carrying out in an organism catalytical function refer to:
The proteins which are carrying out in an organism catalytical function refer to:
During mutation of hemoglobin gene glutamic acid is substituted by another one and this results in sickle-cell anemia. Which amino acid will be occured in the hemoglobin instead of glutamic acid resulting in this disease?
During mutation of hemoglobin gene glutamic acid is substituted by another one and this results in sickle-cell anemia. Which amino acid will be occured in the hemoglobin instead of glutamic acid resulting in this disease?
Vitellin contains:
Vitellin contains:
Monomers of Nucleic acids are:
Monomers of Nucleic acids are:
The spatial orientation of a polypeptide chain containing alpha helices, beta structures, and areas without a periodic structure is called:
The spatial orientation of a polypeptide chain containing alpha helices, beta structures, and areas without a periodic structure is called:
Individual polypeptide chains of oligomeric proteins are called:
Individual polypeptide chains of oligomeric proteins are called:
The number and order of the compound of protomers in a protein is called:
The number and order of the compound of protomers in a protein is called:
In medical practice, denaturing agents are used to sterilize medical instruments in autoclaves. To provide a denaturing agent:
In medical practice, denaturing agents are used to sterilize medical instruments in autoclaves. To provide a denaturing agent:
Fibrillar proteins as opposed to globular:
Fibrillar proteins as opposed to globular:
Hydration of proteins is a:
Hydration of proteins is a:
Protein denaturation is a process in which:
Protein denaturation is a process in which:
Immunoglobulins by chemical nature are:
Immunoglobulins by chemical nature are:
The main function of histones is:
The main function of histones is:
The polypeptide portion of a complex protein is called:
The polypeptide portion of a complex protein is called:
The non-amino acid portion of a complex protein is called:
The non-amino acid portion of a complex protein is called:
Proteins that perform mainly structural function include,:
Proteins that perform mainly structural function include,:
Hormonal function these proteins perform:
Hormonal function these proteins perform:
The transport function of these proteins performs:
The transport function of these proteins performs:
The protective function of these proteins performs:
The protective function of these proteins performs:
Contractile function of these proteins performs:
Contractile function of these proteins performs:
4 types of Collagen are known. Show 1 type of Collagen.
4 types of Collagen are known. Show 1 type of Collagen.
Which amino acids participate to formation of ester bonds between amino acid and phosphoric acid?
Which amino acids participate to formation of ester bonds between amino acid and phosphoric acid?
HbS (sickle cell hemoglobin)
HbS (sickle cell hemoglobin)
Hemoglobins of vertebrate erythrocytes perform two major transport functions: transport of O2 from lungs to peripheral tissues and transport of CO2 and protons from peripheral tissues to lungs.
Hemoglobins of vertebrate erythrocytes perform two major transport functions: transport of O2 from lungs to peripheral tissues and transport of CO2 and protons from peripheral tissues to lungs.
Hemoglobin participates. Show wrong answer:
Hemoglobin participates. Show wrong answer:
Myoglobin - red muscle tissue myoglobin stores oxygen that under conditions of oxygen deprivation (e.g., serve exercise) is released for use by muscle mitochondria for oxygen-dependent synthesis of ATP. Consist of _____ amino acids:
Myoglobin - red muscle tissue myoglobin stores oxygen that under conditions of oxygen deprivation (e.g., serve exercise) is released for use by muscle mitochondria for oxygen-dependent synthesis of ATP. Consist of _____ amino acids:
Transferrin is
Transferrin is
Ferritin is another protein that is important in the metabolism of iron. Under normal conditions, it stores iron that can be called upon for use as conditional require. In conditions of excess of iron
Ferritin is another protein that is important in the metabolism of iron. Under normal conditions, it stores iron that can be called upon for use as conditional require. In conditions of excess of iron
This protein has a blue color because of its high copper content and carries 90% of the copper present in plasma.
This protein has a blue color because of its high copper content and carries 90% of the copper present in plasma.
How much carbohydrates are contained in the structure of glycoproteins?
How much carbohydrates are contained in the structure of glycoproteins?
The representatives of proper (true) GP are......Show wrong answer:
The representatives of proper (true) GP are......Show wrong answer:
These are proteins of slime is contained in a saliva (they provide high viscosity of one), promoting of covering of the food, in a secret of all glands of gastro-intestenal tract, respiratory ways, urine sexual system where they carry out a protective role, in slime of fish, frogs and other reptiles, where they protect a surface of body from the harmful external factors.
These are proteins of slime is contained in a saliva (they provide high viscosity of one), promoting of covering of the food, in a secret of all glands of gastro-intestenal tract, respiratory ways, urine sexual system where they carry out a protective role, in slime of fish, frogs and other reptiles, where they protect a surface of body from the harmful external factors.
Carbohydrates of proteoglycans
Carbohydrates of proteoglycans
There are 6 types of glucosaminoglycans: Find wrong answer:
There are 6 types of glucosaminoglycans: Find wrong answer:
Nucleoproteins in an organism:
Nucleoproteins in an organism:
Nucleoproteins consist of:
Nucleoproteins consist of:
Mononucleotides are:
Mononucleotides are:
What isn't the importance of nucleotides? They
What isn't the importance of nucleotides? They
Adenylic acid enters the
Adenylic acid enters the
Thymidine monophosphate is a component of
Thymidine monophosphate is a component of
Flashcards
Tertiary protein structures
Tertiary protein structures
Ionic, Hydrogen, hydrophobic interactions and disulfide bonds participate in formation of tertiary structure of proteins. Coordination bonds do not.
Casein protein class
Casein protein class
Casein belongs to the class of phosphoproteins.
Non-protein amino acid
Non-protein amino acid
Beta-alanine is an amino acid that is not found in the structure of proteins.
The imino acid
The imino acid
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Sulfur-containing amino acid
Sulfur-containing amino acid
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Hemoglobin's quaternary structure
Hemoglobin's quaternary structure
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Basic nucleoproteins
Basic nucleoproteins
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Nucleic acid function
Nucleic acid function
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Catalytic proteins
Catalytic proteins
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Sickle-cell anemia mutation
Sickle-cell anemia mutation
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Vitellin composition
Vitellin composition
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Nucleic acid monomers
Nucleic acid monomers
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Protein tertiary structure
Protein tertiary structure
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Oligomeric protein subunits
Oligomeric protein subunits
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Protein protomer arrangement
Protein protomer arrangement
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Denaturing agents
Denaturing agents
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Fibrillar vs. globular proteins
Fibrillar vs. globular proteins
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Protein hydration
Protein hydration
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Protein denaturation
Protein denaturation
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Immunoglobulin classification
Immunoglobulin classification
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Study Notes
Tertiary Structure of Proteins
- Coordination bonds are not involved in the creation of the tertiary structure of proteins; ionic, hydrogen, hydrophobic interactions, and disulfide bonds are.
Casein
- Casein is a phosphoprotein.
Amino Acids
- Beta-alanine is not part of the structure of protein molecules.
- Proline is an imino acid.
- Methionine is an amino acid containing sulfur.
Hemoglobin
- The formula for the quaternary structure of a hemoglobin molecule is alfa2beta2.
Nucleoproteins
- Histones are basic simple proteins of human nucleoproteins.
Nucleic Acids Function
- Nucleic acids preserve and transfer genetic information and synthesize proteins.
Catalytical Function
- Enzymes carry out an organism's catalytical functions.
Hemoglobin Mutation
- Valine occurs in hemoglobin instead of glutamic acid, resulting in sickle-cell anemia during mutation of the hemoglobin gene.
Vitellin
- Vitellin contains lipids.
Nucleic Acids
- Nucleotides are monomers of nucleic acids.
Polypeptide Chain Spatial Orientation
- The spatial orientation of a polypeptide chain containing alpha-helices, beta-structures, and areas without a periodic structure is called tertiary structure.
Oligomeric Proteins
- Individual polypeptide chains of oligomeric proteins are called protomers.
Protein Structure
- The number and order of the protomers in a protein compound is called the quaternary structure.
Denaturing Agents
- Alcohol is a denaturing agent utilized to sterilize medical instruments in autoclaves.
Fibrillar Proteins
- Fibrillar proteins have asymmetric (uneven) amino acid composition, as opposed to globular proteins.
Hydration of Proteins
- The hydration of proteins is forming an aqueous shell due to uncharged polar and ionogenic groups on the protein's surface.
Protein Denaturation
- Protein denaturation involves violating the native protein conformation.
Immunoglobulins
- Immunoglobulins are glycoproteins by chemical nature.
Histones
- Histones stabilize the spatial structure of DNA and regulate gene expression.
Complex Protein
- The polypeptide portion of a complex protein is called an apoprotein and the non-amino acid portion is called a prosthetic group.
Structural Function Proteins
- Collagen, scleroproteins, and keratin mainly perform structural functions.
Hormonal Function Proteins
- Insulin performs a hormonal function.
Transport Function Proteins
- Hemoglobin and albumin perform a transport function.
Protective Function Proteins
- Interferon performs a protective function.
Contractile Function Proteins
- Myosin performs a contractile function.
Collagen Types
- Collagen type 1 is contained in greatest quantity in the organism, meeting in the skin, tendons, bones, and cornea.
- Collagen type 4 exists in the cardiovascular system.
Ester Bonds
- Serine, threonine, and tyrosine participate in forming ester bonds between amino acids and phosphoric acid.
Sickle Cell Hemoglobin
- α2$2 represents sickle cell hemoglobin.
Hemoglobin Functions
- Hemoglobin in vertebrate erythrocytes transports O2 from lungs to peripheral tissues and CO2 and protons from peripheral tissues to lungs.
Hemoglobin
- Hemoglobin does not act as a source of bile.
Myoglobin
- Myoglobin consists of 153 amino acids.
Transferrin
- Transferrin is B1-globulin with a molecular mass of approximately 76 kDa.
Iron Storage
- Hemochromatosis occurs under conditions of excess iron with Ferritin.
Copper in Plasma
- Ceruloplasmin has a blue color due to its high copper content and carries 90% of the copper present in plasma.
Glycoproteins
- Glycoproteins contain more than 10% carbohydrates.
True GP Representatives
- HbF, Mg, HbA, and HbB are not true GP representatives.
Saliva Proteins
- Musine is a protein of slime contained in saliva.
Proteoglycans
- Glycosaminoglycans, or mucopolysaccharides, are carbohydrates of proteoglycans.
Glucosaminoglycans
- Musine is not a type of glucosaminoglycan.
Nucleoproteins Functions
- Nucleoproteins carry out a structural function in an organism.
Nucleoproteins Composition
- Nucleoproteins consist of simple proteins and nucleic acids.
Mononucleotides
- Mononucleotides are structural units of polynucleotides.
Nucleotides
- Nucleotides are not components of carbohydrates.
Acids
- Adenylic acid enters RNA.
Thymidine Monophosphate
- Thymidine monophosphate is a component of DNA.
Nucleotides of DNA
- Nucleotides of DNA are not part of phosphoproteins.
Nucleoside Triphosphate Importance
- A nucleoside triphosphate is a component of nucleotides.
Complementarity
- Complementarity is characteristically for A and T.
Complementarity Principle
- The principle of complementarity is characteristic of DNA.
DNA Molecules
- Changeable quantity is characteristic of DNA molecules.
DNA Primary Structure
- The primary structure of DNA is determined by a chain of maternal DNA.
- Phosphodiester bond stabilizes the primary structure of DNA.
- The primary structure of DNA is represented by a one-spiral polynucleotide chain.
DNA Secondary Structure
- The secondary structure of DNA is represented by a two-spiral polynucleotide chain, observing Chargaff's rules.
- Hydrogen, forces Van der Waals, and ionic bonds stabilize the secondary structure of DNA.
DNA Tertiary Structure
- The tertiary structure of DNA is a nucleosoma.
DNA Quaternary Structure
- The quaternary structure of DNA is a chromosome.
RNA vs. DNA
- RNA differs from DNA because it is not submitted to rules Chargaff.
Primary Structure of RNA
- The primary structure of RNA is a one-spiral polynucleotide chain.
mRNA
- The secondary structure of mRNA is represented by free loops.
tRNA
- tRNA recognizes amino acids and carries them to a ribosome.
tRNA Specificity
- The structure of aminoacyl-tRNA synthetase provides the specificity of tRNA to a particular amino acid.
tRNA Coding
- The structure of aminoacyl-tRNA synthetase provides specificity of t-RNA to a determined codon.
Antycodone
- Antycodone is located on t-RNA
DNA
- Deoxyribose is a monosaccharide component of nucleotides in DNA.
Maltose
- Maltose has an α(1→4) glycosidic bond.
Carbohydrates
- Glycogen is a storage form of carbohydrates in animals.
- Lactose is known as milk sugar.
- Sucrose is a non-reducing sugar.
Plant Cell Walls
- Cellulose is a major component of plant cell walls.
Heteropolysaccharide
- Hyaluronic acid is a heteropolysaccharide.
Bacterial Cell Walls
- N-acetylglucosamine is involved in the structure of bacterial cell walls.
Animal Starch
- Glycogen is known as animal starch.
Dietary Fiber
- Reducing glucose and cholesterol absorption is the main function of dietary fiber in human nutrition.
Kidney Function
- Inulin is used to assess kidney function.
Aldohexose
- Glucose is an aldohexose.
Sucrose
- Sucrose contains an α(1-2) β glycosidic bond.
Sugar Alcohol
- Sorbitol is a sugar alcohol.
Humans Digestion
- Cellulose cannot be digested in humans.
Sweetest Sugar
- Fructose is the sweetest naturally occurring sugar.
Carbohydrate Molecular Breakdown
- Starch hydrolyzes to yield only glucose molecules.
Marathon Energy
- Glycogen will be primarily utilized as an energy source during a marathon.
Disrupting Lactase
- Disrupting the enzyme lactase results in lactose intolerance.
Glycosaminoglycans
- The structural integrity of connective tissue demonstrates the importance of glycosaminoglycans (GAGs) in human physiology.
Energy Storage
- Lipids are the primary storage form of energy in the body.
Cell Membranes
- Phospholipids are the main component of cell membranes.
Lipids
- Lipids function as Enzymes for catalysis.
- Saturated fatty acids contain no double bonds.
- Saturated fatty acids increase LDL cholesterol levels.
Fatty acids
- Trans fatty acids have hydrogen atoms opposite the sides of the double bond.
- Omega-3 fatty acids act as an anti-inflammatory agent.
Cholesterol Transport
- LDL is primarily responsible for transporting cholesterol from the liver to other tissues.
Derivatives
- Eicosanoids are a derivative of polyenoic fatty acids.
Steroid Hormones
- Cholesterol is the precursor for steroid hormones.
Good Cholesterol
- HDL is known as "good cholesterol".
Essential Fatty Acid
- Linoleic acid is an essential fatty acid and must be obtained from the diet.
Lipids Classes
- Glycolipids include cerebrosides and gangliosides classes of lipids.
Trans Fatty Acids
- Trans-fatty acids increase the risk of cardiovascular diseases.
Cell Signaling
- Phospholipids play a role in cell signaling.
Dietary Triglycerides
- Chylomicrons are synthesized in the intestine and transport dietary triglycerides.
Bile Acids
- Cholesterol is a major component of bile acids.
Lower Cholesterol
- Saturated fats should be minimized to decrease LDL cholesterol levels in patients with atherosclerosis.
Hydrogenation
- Trans-unsaturated fatty acids are most likely increased when hydrogenating vegetable oil.
Lipid Absorption
- Bile acid deficiency impairs cholesterol absorption in newborns.
Omega-3 Supplements
- Omega-3 fatty acids reduce serum triglyceride levels by decreasing VLDL synthesis.
Lipid Study Focus
- Arachidonic acid is the lipid essential for the synthesis of eicosanoids.
Trans Fats
- Elevated C-reactive protein levels are likely to occur when increasing trans fats.
Lipid Molecules
- A lipid molecule composed of glycerol, two fatty acids, and a phosphate group is most likely involved in cell membrane structure.
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