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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
- Ionic bond
- disulfide bond
- Coordination bond (correct)
- Hydrogen bond
Casein concerns to a class of:
Casein concerns to a class of:
- chromoproteins
- lipoproteins
- phosphoproteins (correct)
- glycoproteins
- 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
- glutamic 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:
Which class of enzymes includes respiratory enzymes?
Which class of enzymes includes respiratory enzymes?
Enzymes of digestion belong to a class:
Enzymes of digestion belong to a class:
How enzymes do accelerate reactions:
How enzymes do accelerate reactions:
A temperature optimum for the majority of enzymes is:
A temperature optimum for the majority of enzymes is:
Which of following factors doesn't influence on enzymatic reactions?
Which of following factors doesn't influence on enzymatic reactions?
Reactions of nonhydrolytic cleavage or connection on the site of double bond are catalyzed by:
Reactions of nonhydrolytic cleavage or connection on the site of double bond are catalyzed by:
Competitive inhibitors:
Competitive inhibitors:
The enzymes influencing on certain substrate and catalyzing the same reaction with this substrate, but distinguish on physical and chemical properties refer to:
The enzymes influencing on certain substrate and catalyzing the same reaction with this substrate, but distinguish on physical and chemical properties refer to:
Which class of enzymes does chymotrypsin belong to?
Which class of enzymes does chymotrypsin belong to?
Enzyme, catalyzing splitting of H2O2 to water and oxygen belong to:
Enzyme, catalyzing splitting of H2O2 to water and oxygen belong to:
Cytochromes concern to a class of:
Cytochromes concern to a class of:
Where do oxidative phosphorylations occur?
Where do oxidative phosphorylations occur?
What is the multienzymic complex?
What is the multienzymic complex?
The control of breath is carried out by:
The control of breath is carried out by:
The basic function of the fourth respiratory complex is transfer of electrons from cytochrome to:
The basic function of the fourth respiratory complex is transfer of electrons from cytochrome to:
Lactatedehydrogenase-1 (LDH1) occurs in
Lactatedehydrogenase-1 (LDH1) occurs in
Glutathione peroxidase contains the following metal:
Glutathione peroxidase contains the following metal:
Coenzyme of cocarboxylase-is:
Coenzyme of cocarboxylase-is:
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:
The active center of the one-component enzyme is formed:
The active center of the one-component enzyme is formed:
Complex two-component enzymes have a non-protein part called:
Complex two-component enzymes have a non-protein part called:
The second stage of enzymatic catalysis is:
The second stage of enzymatic catalysis is:
Allosteric center of the enzyme is:
Allosteric center of the enzyme is:
An example of a drug is a structural analog of paraaminobenzoic acid, from which H4 (folate) is synthesized in a microorganism cell, participating in the biosynthesis of nitrogenous bases
An example of a drug is a structural analog of paraaminobenzoic acid, from which H4 (folate) is synthesized in a microorganism cell, participating in the biosynthesis of nitrogenous bases
The basis of the action of some toxic substances is the inhibition of enzyme activity, for example, compounds:
The basis of the action of some toxic substances is the inhibition of enzyme activity, for example, compounds:
Enzymes that catalyze hydrolytic decomposition reactions belong to the class:
Enzymes that catalyze hydrolytic decomposition reactions belong to the class:
Enzymes that catalyze the cleavage from substrates of certain groups in a nonhydrolytic way with the formation of a double bond belong to the class:
Enzymes that catalyze the cleavage from substrates of certain groups in a nonhydrolytic way with the formation of a double bond belong to the class:
Flashcards
Non-participating bond
Non-participating bond
Coordination bonds do not participate in forming the tertiary structure of proteins.
Casein class
Casein class
Casein belongs to the class of phosphoproteins.
Non-protein amino acid
Non-protein amino acid
Beta-alanine is not found in the structure of proteins. It is a non-protein amino acid.
Imino acid
Imino acid
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Sulfur-containing amino acid
Sulfur-containing amino acid
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Hemoglobin formula
Hemoglobin formula
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Basic nucleoprotein
Basic nucleoprotein
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Function of Nucleic Acids
Function of Nucleic Acids
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Catalytical proteins
Catalytical proteins
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Amino acid change
Amino acid change
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Vitellin contains:
Vitellin contains:
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Monomers of Nucleic Acids
Monomers of Nucleic Acids
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Respiratory enzyme class
Respiratory enzyme class
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Digestion Enzyme Class
Digestion Enzyme Class
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Reaction acceleration
Reaction acceleration
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Optimum temperature
Optimum temperature
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Factors doesn't influence enzymatic reactions
Factors doesn't influence enzymatic reactions
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Nonhydrolytic cleavage catalysts
Nonhydrolytic cleavage catalysts
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Competitive inhibitors
Competitive inhibitors
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Enzyme variants
Enzyme variants
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Study Notes
- Coordination bonds do not participate in the formation of the tertiary structure of proteins.
- Casein belongs to the class of phosphoproteins.
- Beta-alanine is an amino acid not found in the structure of protein molecules.
- Proline represents an imino acid.
- Methionine is an amino acid that contains sulfur.
- The quaternary structure of hemoglobin is described by the formula alfa2beta2.
- Protamine, albumins, and histones represent basic nucleoproteins in humans.
- Nucleic acids function in the preservation and transfer of genetic information, as well as the synthesis of proteins.
- Enzymes facilitate catalytic functions within an organism.
- Mutation of the hemoglobin gene where glutamic acid is substituted results in sickle-cell anemia.
- Valine will occur in hemoglobin instead of glutamic acid, resulting in sickle-cell anemia.
- Vitellin contains lipids.
- Nucleotides are monomers of nucleic acids.
- Oxidoreductases encompass the class of respiratory enzymes.
- Hydrolases represent the class of digestive enzymes.
- Enzymes accelerate reactions by lowering the energy of activation
- The optimum temperature for most enzymes falls within 36-45°C.
- The nature of the enzyme is not a factor that influences enzymatic reactions.
- Reactions involving nonhydrolytic cleavage or connection at a double bond site are catalyzed by lyases.
- Competitive inhibitors contact with the active center of an enzyme.
- Isoenzymes influence a certain substrate and catalyze the same reaction, but they possess distinct physical and chemical properties.
- Chymotrypsin is classified as a hydrolase.
- Catalase is the enzyme responsible for catalyzing the splitting of H2O2 into water and oxygen.
- Cytochromes are classified as oxidoreductases.
- Oxidative phosphorylation occurs in the mitochondria.
- Multienzymic complexes represent a group of enzymes that possess various specificities of action.
- The concentration of malate controls breath.
- The basic function of the fourth respiratory complex involves transferring electrons from cytochrome to oxygen.
- Lactate dehydrogenase-1 (LDH1) is predominantly found in the heart.
- Glutathione peroxidase contains the metal selenium.
- Cocarboxylase has thiamine pyrophosphate as its coenzyme.
- The spatial orientation of a polypeptide chain containing alpha helices, beta structures, and areas without a periodic structure is referred to as the tertiary structure.
- Protomers are individual polypeptide chains of oligomeric proteins.
- The number and order of the compound of protomers in a protein is called its quaternary structure.
- Alcohols serve as denaturing agents used in medical practice to sterilize medical instruments in autoclaves.
- Fibrillar proteins - as opposed to globular - do not have complex spatial packaging.
- Hydration of proteins involves the formation of an aqueous shell due to the presence of uncharged polar and ionogenic groups on the surface of the protein
- Protein denaturation is a process in which the native protein conformation is lost.
- Immunoglobulins are, by chemical nature defined as glycoproteins.
- Binding and stabilization of the spatial structure of DNA and regulation of gene expression are the main function of histones.
- A polypeptide portion of a complex protein is known as an apoprotein.
- The non-amino acid portion of a complex protein is referred to as a prosthetic group.
- Collagen and myosin are proteins that perform mainly structural functions.
- Insulin facilitates the hormonal function in proteins.
- Hemoglobin performs a transport function.
- Interferon enables a protective function through proteins.
- Myosin is a protein that enables the contractile function.
- Radicals of mainly amino acid residues form the active center of a one-component enzyme
- Complex two-component enzymes have a non-protein part referred to as a cofactor.
- The creation of the enzyme-substrate complex is the second stage of enzymatic catalysis.
- Breaking the reaction product down from the enzyme is the third stage of enzymatic catalysis.
- A set of functional groups on the enzyme's surface that interacts with effectors defines the allosteric center of an enzyme.
- An example of a drug is a structural analog of para-aminobenzoic acid, from which H4 (folate) is synthesized in a microorganism cell, participating in the biosynthesis of nitrogenous bases
- Many toxic substances inhibit enzyme activity.
- Hydrolases belong to the class of enzymes that catalyze hydrolytic decomposition reactions.
- Lyases belong to the class of enzymes that catalyze the cleavage from substrates of certain groups in a nonhydrolytic way with the formation of a double bond.
- Isomerases catalyze the reaction of intramolecular transfer of chemical groups
- Ligases are the class of enzymes that catalyze the connection of two molecules- coupled with the cleavage of the macroerhic bond in the ATP molecule.
- A gene defect or gene expression is the cause of hereditary enzymopathies.
- Exposure to toxic substances will cause toxic enzymopathies.
- The ability of enzymes to maintain their activity outside the human body will allow a basis of enzymodiagnostics.
- Hydrolases include Tripsin, pepsin, and catepsin.
- Dynamic functions include transformations, transport, metabolic control, and contraction
- There are 4 known types of collagen, one being contained in an organism in the greatest quantity, which meets in skin, tendons, bones, cornea.
- Shows the second type of collagen met in intima of vessels and cardiovascular system.
- Shows fourth type of collagen that contains that meet in cartilages or the glassoid body of an eye.
- Nuclease are in the hydrolase class.
- The main mechanism for regulating enzyme activity is controlled through metabolic pathways
- There are the following types of phosphoproteins that shows milk casein(ogen) is with (P~ 1%).
- Serine, threonine, and tyrosine amino acids participate in forming ester bonds between amino acids and phosphoric acid.
- Hemoglobin or HbS with (sickle cell hemoglobin) has the formula α2β2.
- Hemoglobins of vertebrate blood cells perform two major transport functions, for O2 from lungs to peripheral tissues and transport of CO2 and protons from peripheral tissues to lungs.
- Hemoglobin does not participate as forming a source of bile.
- 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 and consists of 153 amino acids
- Transferrin is B1-globulin with a molecular mass of approximately 76 kDa.
- Ferritin - under normal conditions, it stores iron that can be called upon for use, which requires more conditional iron called Hemochromatosis. Ceruloplasmin holds a protein with a blue color because of its high copper content and carries 90% of our plasma's existing copper levels.
- More than 5% of carbohydrates are contained in the structure of glycoproteins
- All the representatives of proper/ true GP or sialoproteins, hormones, protrombin, transcortin, ceruloplasmin, haptoglobin protein of blood's, group specificity, immunoglobulins, nor mucins
- These -proteins of slime are contained in saliva - they provide high viscosity of one -promoting covering of the food and in a secretion of all glands of gastro intestinal 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
- Sialic acid is a carbohydrate of proteoglycans
- Musine there are 6 types of glucosaminoglycans
- Is a quantity of molecules of enzymes on which -the one molecule of enzymes acts during1 minute The next property of high enzymes activates. The activity is measured in catal.
- Shows substrate specificity named “absolute” with Succinate dehydrogenase to fumarate
- SHOWs two-types of enzymes:
- Specificity: amylase starch and glycogen
- Non-competitive inhibition - enzyme cytochrome oxidase with non-competitive inhibition
- Carboxypeptidase with conjugated proteins and Zinc is a coenzyme.
- The lipase of pancreatic juice is secreted by pancreatic cells in inactive form - one that is only activated by conjugated salts of Bile acid.
- The urokinase and streptokinase that show used lysis of blood clots/ i.e in thrombophlebitis and aminotransferases consist of - apoenzyme +coenzyme?
- The following Acyltransferases -apoenzyme + Coenzyme
- Which only consist B2
- The only source thiamine shows enzyme participating in the reactions of protein synthesis.
- Alfa-ketoglutaric acid + aspartic acid is a way to have oxaloacetic acid as an enzymatic reaction.
- The importance in Methyltransferases is to catalyze the methylation . Vitamin B12 helps the reaction forming
- The only source 3 Glycine in Ethanolamine
- There are five functions for nucleoproteins in the organism:
- Protective
- Water metabolism
- Structural -Tissue specificity -Transport
- The only acid that nucleic and simple nucleoproteins contain is the rest of phosphoric acids.
- The structural units of mononucleotides are that they consist of polynucleotide.
- There will be sources of formation of nucleoside triphosphate in the function of nucleotides. Adenylic acid should enter -RNA
- DNA and RNA need Thymidine monophosphate as its components
- There must be-enters of DNA in Nucleotides, and they are not part of DNA at all. -Nucleoside triphosphate should have a great importance as its an source for phosphoric acid and energy is still necessary for the synthesis of proteins + participates in forming nucleic acids or in a component of nucleotide.
- Complementarity happens characteristically with the two molecules A and G
- From the listed molecules protein cannot be applied from the principle of having -molecular complementarity For a molecule DNA cant be changeable quantity: The rules follow constant quantity of molecule that has to big a molecular weight for observance of rules from Chargaff
- Primary structures of any kind of DNA are usually determined by: having to link polymerase
- As showing to exist on a molecule -Primary structure will not happen on molecules by disulfide bond.
- To show where should primary structure of our known DNA be represented :Two -spiral polynucleotide.
- There happens with observances of the rules for the type of DNA - which only happens with chain
- By known to showing which structures are best for the types of DNA + show the known chains , which secondary structure DNA might come stabilized by: force Van der Waals
- Secondary must show no support +
Tertiary with any structures from loop showing to exist on a free chain showing to be best +closed : with chromosome. - To know what is the difference to any -RNA - this that is from the submitted rules from Chargaff-big molecular weight +has one polynucleotide chain &has not changeable quantity
- Now the function with structures that exist around the molecules of -Now to show to knowing what happens when molecules show differences
- To show which different types exist + what functions exist between these different molecuels that have to be able to form around us . t -RNA must carry amino acids through amino acids form on ribosome to form to transport the from -DNA amino to from its ribosome. To know how To known structures of molecular functions show specificity t-RNA with these amino acids. To show what is from amino aicds + tRNA with spatial conformity + To show where known from from -DNA to with a ribosome .
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