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Questions and Answers
Which of the following bonds don't participate in formation of tertiary structure of proteins?
Which of the following bonds don't participate in formation of tertiary structure of proteins?
- disulfide bond
- Coordination bond (correct)
- Ionic bond
- hydrophobic interactions
- Hydrogen bond
Casein concerns to a class of:
Casein concerns to a class of:
- phosphoproteins (correct)
- chromoproteins
- lipoproteins
- metalloproteins
- glycoproteins
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:
- phenylalanine
- lysine
- proline
- glytamic acid
- beta-alanine (correct)
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
Nucleotides of DNA aren't
Nucleotides of DNA aren't
Nucleoside triphosphate has a great importance because it isn't
Nucleoside triphosphate has a great importance because it isn't
Flashcards
Tertiary structure of proteins
Tertiary structure of proteins
Includes ionic, hydrogen, hydrophobic interactions and disulfide bonds.
Phosphoproteins
Phosphoproteins
Proteins that contain phosphorus as a prosthetic group.
Non-protein amino acid example
Non-protein amino acid example
Beta-alanine is not a standard amino acid in protein structures.
Imino acid
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 simple proteins of nucleoproteins
Basic simple proteins of nucleoproteins
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Function of nucleic acids
Function of nucleic acids
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Catalytic proteins
Catalytic proteins
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Amino acid substitution in sickle cell
Amino acid substitution in sickle cell
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Vitellin content example
Vitellin content example
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Monomers of nucleic acids
Monomers of nucleic acids
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Spatial orientation of polypeptide chain
Spatial orientation of polypeptide chain
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Protomer
Protomer
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Primary structure
Primary structure
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Denaturing agent for sterilization example
Denaturing agent for sterilization example
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Fibrillar proteins properties
Fibrillar proteins properties
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Definition of protein denaturation
Definition of protein denaturation
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Main function of histones
Main function of histones
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Polypeptide portion of a complex protein
Polypeptide portion of a complex protein
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Study Notes
- Ionic, hydrogen, hydrophobic interactions, and disulfide bonds participate in the formation of tertiary structures of proteins; coordination bonds do not.
- Casein belongs to the class of phosphoproteins.
- Beta-alanine is not a typical amino acid found in protein structures.
- Proline is classified as an imino acid.
- Methionine is the amino acid that contains sulfur.
- The quaternary structure of hemoglobin is described by the formula α2β2.
- Histones are basic simple proteins found in human nucleoproteins.
- The main function of nucleic acids involves preservation and transfer of genetic information, along with protein synthesis.
- Enzymes are proteins that perform a catalytic function in organisms.
- In sickle-cell anemia, glutamic acid is substituted by valine in the hemoglobin gene.
- Vitellin contains lipids.
- Nucleotides are the monomers of nucleic acids.
- The spatial orientation of a polypeptide chain with alpha helices, beta structures, and areas without a periodic structure is called tertiary structure.
- Individual polypeptide chains of oligomeric proteins are called protomers.
- Determination of the number and order of protomers in a protein is called quaternary structure.
- Denaturing agents, such as high temperature, acids, alkalis, heavy metal salts and alcohol, are used to sterilize medical instruments in autoclaves.
- Fibrillar proteins, as opposed to globular ones, have asymmetric (uneven) amino acid composition.
- Hydration of proteins involves the formation of an aqueous shell around the protein due to polar and ionogenic groups on its surface.
- Protein denaturation is a process in which the native conformation of the protein is disrupted.
- Immunoglobulins are glycoproteins by chemical nature.
- The primary function of histones includes stabilization of the spatial structure of DNA and regulation of gene expression.
- The polypeptide portion of a complex protein is called an apoprotein.
- The non-amino acid portion of a complex protein is called a prosthetic group.
- Collagen, keratin, scleroproteins and myosin are proteins that mainly perform structural functions.
- Insulin performs a hormonal function.
- Hemoglobin performs a transport function.
- Albumin, interferon, actin, insulin and myosin perform a transport function.
- Actin, interferon, insulin, albumin and myosin perform a protective function.
- Myosin performs a contractile function.
- Collagen is contained in the greatest quantity in the organism.
- Alanine, valine and tryptophan can participate in the formation of ester bonds between amino acids and phosphoric acid.
- Serine, threonine and tyrosine will participate in the formation of ester bonds between amino acid and phosphoric acid?
- HbS (sickle cell hemoglobin) is α2β2
- Hemoglobins of vertebrate erythrocytes transport O₂ from the lungs to peripheral tissues and CO₂ and protons from peripheral tissues to the lungs.
- Hemoglobin does not act as a source of bile.
- Myoglobin is a red muscle tissue that stores oxygen released for ATP synthesis during oxygen deprivation.
- Myoglobin consists of 153 amino acids.
- Transferrin is a β₁-globulin with a molecular mass of approximately 76 kDa.
- Ferritin stores iron for conditional use and can indicate hemochromatosis in cases of excess iron.
- Ceruloplasmin has a blue color due to its high copper content and carries 90% of the copper in plasma.
- Glycoproteins contain more than 5% of carbohydrates in their structure.
- Sialoproteins and hormones are not considered as components of proper (true) GP
- Proteins of slime contained in saliva are musine, sialic acid, fucose, galactose and neuraminic acid.
- Carbohydrates of proteoglycans are glycosaminoglycans or mucopolysaccharides.
- Musine is not a type of glucosaminoglycan.
- Nucleoproteins in an organism carry out protective and structural functions as well as providing specificity of tissues.
- Nucleoproteins consist of simple proteins and nucleic acids.
- Mononucleotides are structural units of polynucleotides.
- Nucleotides are not components of carbohydrates.
- Adenylic acid enters the RNA and DNA.
- Thymidine monophosphate is a component of DNA.
- Nucleotides of DNA aren't part of phosphoproteins.
- Nucleoside triphosphateis not a component of nucleotides.
- Complementarity is characteristically for adenine and thymine.
- The principle of complementarity is characteristic of DNA, m-RNA, t-RNA and r-RNA.
- For molecules of DNA, changeable quantity is not characteristic.
- The primary structure of DNA is determined by nucleosoma.
- Primary structure of DNA is stabilized by phosphodiester bonds.
- The primary structure of DNA is represented by one-spiral polynucleotide chain.
- Secondary structure of DNA is represented by two-spiral polynucleotide chain with observance of rules Char gaff.
- Secondary structure of DNA is not stabilized by ionic.
- Tertiary structure of DNA is nucleosoma.
- Quarternary structure of DNA is chromosome.
- RNA differs from DNA because it has one polynucleotide chain.
- The primary structure of RNA is one-spiral polynucleotide chain.
- The secondary structure of m-RNA is represented by free loops.
- The role of t-RNA is to recognize amino acids and carry them to a ribosome.
- The specification of t-RNA to certain amino acid is provided by the structure of aminoacyl-tRNA synthetase.
- Especificity t-RNA to determined codon is provided by place of an attachment to a ribosome..
- Antycodone is located on t-RNA.
- Deoxyribose is a component of nucleotides in DNA.
- Maltose has an α(1→4) glycosidic bond.
- Glycogen serves as a storage form of carbohydrates in animals.
- Lactose is known as milk sugar.
- Sucrose is a non-reducing sugar.
- Cellulose is a major component of plant cell walls.
- Hyaluronic acid is a heteropolysaccharide.
- N-acetylglucosamine is involved in the structure of bacterial cell walls.
- Glycogen is known as animal starch.
- Reducing glucose and cholesterol absorption is the main function of dietary fiber in human nutrition.
- Inulin is a carbohydrate used for assessing kidney function.
- Glucose is an aldohexose.
- α(1-2) β is the glycosidic bond present in sucrose.
- Sorbitol is a sugar alcohol.
- Cellulose carbohydrate cannot be digested by humans.
- Fructose is the sweetest naturally occurring sugar.
- Starch yields only glucose molecules upon hydrolysis, the original composition of the sample by researcher.
- Glycogen will be utilized as an energy source during the marathon race.
- Lactose intolerance is the most likely consequence of mutation disrupts the enzyme lactase
- Structural integrity of connective tissue demonstrates the importance of glycosamino glycans (GAGs) in human physiology.
- Lipids are the primary storage form of energy in the body.
- Phospholipids are the main component of cell membranes.
- Enzyme catalysis is NOT a function of lipids.
- Saturated fatty acids contain no double bonds.
- Saturated fatty acids are known to increase bad LDL cholesterol levels.
- Trans fatty acids have hydrogen atoms on the opposite sides of a double bond.
- Omega-3 fatty acids acts as an anti-inflammatory agent.
- LDL is primarily responsible for transporting cholesterol to cell membranes from the liver to other tissues.
- Eicosanoids are a derivative of polyenoic fatty acids.
- Cholesterol is the precursor for steroid hormones.
- HDL is known as "good cholesterol”.
- Linoleic acid is an essential fatty acid that must be obtained from the diet.
- Glycolipids includes cerebrosides and gangliosides.
- Trans fatty acids are associated with an increased risk of cardiovascular diseases.
- Sterols plays a role in cell signalling of lipids.
- VLDL is synthesized in the intestine and transports dietary triglycerides?
- Cholesterol is a major component of bile acids.
- Reduce your intake of Saturated fats minimizes to decrease the LDL cholesterol levels.
- Trans unsaturated fatty acids is likely increased is when vegetable oil is hydrogenated.
- Absorption of cholesterol in the intestines are most likely to be impaired, leading to issues like newborn bile acid synthesis deficiency.
- Decreased VLDL synthesis is a primary mechanism by which omega-3 fatty acids reduces serum triglyceride levels.
- Arachidonic acid is most likely the focus of the study by researcher for synthesis of eicosanoids.
- Elevated C-reactive protein levels is most likely a physiological change to occur when an individual adopts a diet high in trans fats.
- Cell Membrane structure contains molecule consists of glycerol, two fatty acids, and a phosphate group.
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