Help
Options
Didn't know it?
click below
click below
Knew it?
click below
click below
Don't Know
Remaining cards (0)
Know
retry
shuffle
restart
0:00
Embed Code - If you would like this activity on your web page, copy the script below and paste it into your web page.
Normal Size Small Size show me how
Normal Size Small Size show me how
Biochem sem1
quest
| Question | Answer |
|---|---|
| 1.Describe the nature and relative strength of covalent bonds, ionic interactions, and van der Waals interactions (hydrogen bonds, dipole–dipole interactions, and London dispersion forces). | In relation to each other, covalent bonds are the strongest, followed by ionic, hydrogen bond, Dipole-Dipole Interactions and Van der Waals forces (Dispersion Forces). |
| 2.What is the relationship between polarity and hydrophobicity? | Hydrophobicity is related to polarity because hydrophobic molecules are nonpolar. Hydrophobic molecules do not have full or partial charges and thus do not dissolve in water. Hydrophilic molecules do have charges and can be dissolved in water. |
| 3. Explain why polar substances dissolve in water while nonpolar substances do not. | Polar substances will have charges or poles which cause attraction and thus are soluble but non-polar substances do not have charges or poles so they are insoluble in water. |
| 4. Explain why amphiphiles form micelles or bilayers in water. | Micelles are globules of amphiphilic molecules arranged so that the hydrophilic groups are at the surface and the hydrophobic groups associate at the centre. |
| 5.How does osmosis differ from diffusion? Which process occurs during dialysis? | Osmosis is the diffusion of water molecules across a partially permeable membrane while dialysis can occur through either diffusion or filtration. |
| 6.Describe the osmotic challenges facing a cell placed in pure water or in a high-salt solution. | A cell placed in water will allow water to move inside the cell, causing the cell to burst. On the contrary, a cell placed in concentrated salt solutions will cause water to move out of the cell, causing it to shrink. |
| 7.What are the products of water’s ionisation? How are their concentrations related? | Products of water ionisation = H+ and OH- ions. - In pure water, [H+] = [OH-] - Solution with higher [H+] are considered acidic - Solutions with higher [OH-] are considered basic |
| 8.Describe how to calculate pH from the concentration of H+ or OH−. | By using the formula: pH = - log ([H+]). Or pH = 14 - ( -log ([OH-]) ). (I THINK) |
| 9. Define acid and base. | Acids are below 7 and between 0 on the pH scale whereas bases are above 7 and between 14. Acids release H+ and bases release OH- when dissolved in water |
| 10.What is the relationship between the strength of an acid and its pK value? | The lower the pH, the higher the concentration of hydrogen ions [H+] and vice versa. |
| 11.What is the Ionic product of water? | The Ionic Product of Water, Kw, is the equilibrium constant for the reaction in which water undergoes an acid-base reaction with itself. That is, water is behaving simultaneously as both an acid and a base. |
| 12.Define pH. | A measure of how acidic or basic a substance or solution is. pH is measured on a scale of 0 to 14. On this scale, a pH value of 7 is neutral, which means it is neither acidic nor basic. The pH of a solution is a measure of the concentration of H+ ions |
| 13.Differentiate between an acid and a base. | An acid is any hydrogen-containing substance that is capable of donating a proton (hydrogen ion) to another substance. A base is a molecule or ion able to accept a hydrogen ion from an acid. Acidic substances are usually identified by their sour taste. |
| 14. What are conjugate acids and bases? | a conjugate acid–base pair consists of two substances that differ only by the presence of a proton (H⁺). A conjugate acid is formed when a proton is added to a base, and a conjugate base is formed when a proton is removed from an acid. |
| 15.What is the relative strength of acids and bases? | Strong acids and bases fully ionise in water and weak acids and bases only partially ionises in water |
| 16. What is ionisation constant? | is a value that represents the equilibrium between a substance in its ionised and non-ionized form. For example, consider the ionisation of an acid, HA, in water: HA + H2O → H3O+ + A- |
| 17. Define the Henderson-Hasselbalch Equation. | One way to determine the pH of a buffer is by using the Henderson–Hasselbalch equation, which is pH = pKₐ + log([A⁻]/[HA]). In this equation, [HA] and [A⁻] refer to the equilibrium concentrations of the conjugate acid–base pair used to create the buffer s |
| 18.What are Buffers? | Buffer solutions maintain a stable pH by neutralizing added acids or bases. They consist of a weak acid and its conjugate base, which exchange protons and hydroxide ions to form water. |
| 19.Explain the mechanism how the buffers maintain the constant pH in a solution | Buffer is a mixture of a conjugate acid-base pair that can resist changes in pH when small volumes of strong acids or bases are added. When a strong base is added, the acid present in the buffer neutralizes the hydroxide ions (OH-) When a strong acid is a |
| 20.What are Physiological buffers? Or Describe the physiological importance of buffers. | Physiological buffers are the second line of defence against pH shift. Examples of physiological buffers are: Respiratory mechanism (CO2 excretion) and Renal mechanism (H+ excretion). |
| 21.What is Osmosis? Define osmotic pressure. | Osmosis is the movement of solvent molecules through a semipermeable membrane from an area of low solute concentration to an area of high solute concentration.Osmotic pressure is determined by the concentration of solutes in a solution and the size and ch |
| 22.What are Amino acids? | Amino acids are the monomers that make up proteins. protein is made up of one or more linear chains of amino acids, each of which is called a polypeptide. There are 20 types of amino acids found in proteins. |
| 23. Discuss briefly the Classification of Amino acids. | The 20 amino acids used for protein synthesis are grouped into different classifications according to the polarity and structural features of the side chains. |
| 24. How the amino acids are classified nutritionally? | Essential amino acids-cannot be made by the body Nonessential amino acids-our bodies can produce Conditional amino acids-usually not essential, except in times of illness |
| 25. Mention some important general properties of amino acids. Zwitter ion and Isoelectric pH,Peptide bonds, Isomerism(stoichiometry), Acid base properties | An amino acid can act either as an acid or a base. Amino acids never assume the neutral form in aqueous solution. |
| 26.List important physical properties of amino acids. | Amino acids are colorless, crystalline substance. Amino acids have high melting point |
| 27.Write a note on the role of amino acids as biologically important molecules. | Their primary function is to act as the monomer unit in protein synthesis. |
| 28.What are Proteins? Write some of the important functions of them. | Proteins are composed of one or more linear polypeptide chains containing hundreds of amino acids. provide structure, movement (muscles) |
| 29.Classify proteins on the basis of shape and size. | three types; fibrous, globular and derived protein |
| 30.Classify proteins on the basis of functional properties. | provide structure, movement (muscles) |
| 31.Classify proteins on the basis of solubility and its physical properties. | Fibrous (keratin, collagen, myosin, elastin) proteins are insoluble, globular (albumin, hemoglobin, myoglobin) proteins are soluble. |
| 32.What are simple proteins? Mention some of the important simple proteins | Also known as homoproteins, they are made up of only amino acids. Examples are plasma albumin, collagen, and keratin. |
| 33.What are Conjugated proteins? How they are classified further. | contain in their structure a non-protein portion.Three examples are glycoproteins, chromoproteins, and phosphoproteins. |
| 34. Discuss the Structural Organization of Proteins. Primary,secondary,tertiary ,quaternary-example | primary-sequence amin. aci secondary- helix tetriary-folding quaternary-combi. proteins |
| 35.Discuss few general properties of Proteins. | they have neither acidic nor basic properties. Solubility in Water |
| 36.Mentions the bonds responsible for the formations of protein molecules. | A protein molecule is made from a long chain of amino acids, each linked to its neighbor through a covalent peptide bond. |
| 37.Classify the 20 standard amino acids by polarity, structure, type of functional group,and acid–base properties. | glycine,alanine,proliner, valine, leucine, isoleucine-nonpolar phenylalanine, tyrocine, tryptophan-aromatic asparagine,glutamine, serine, threosine-polar methoionine, cystine-sulfur aspartate, glutamate, arginine, lysine, histidine-charded |
| 38 .Why do the pK values of ionizable groups differ between free amino acids and amino acid residues in polypeptides | The three-dimensional structure of the polypeptide chain brings the polar side chain, carboxyl; amino sides close together due to the electrostatic force of attraction. |
| 39.Explain why all the amino acids except for glycine are chiral.. | Glycine has 2 hydrogens attached to the central carbon so it cannot have any enantiomers |
| 40.Explain how the Fischer convention describes the absolute configuration of a chiral molecule. | configuration of a chiral molecule can be explained by relating its L-stereoisomer with L-glyceraldehyde. Two molecules can be in the same relative configuration if hydroxyl, aldehydic and H groups of glyceraldehyde are the same with a chiral molecule. |
| 41. Explain why an enzyme can catalyze a chemical reaction involving just one enantiomer of a compound. | Enzymes will bind to only one active isomer at a time or can bind separately. Because in most cases, among two enantiomers, only one is active, and the other is inert. |
| 42. List some covalent modifications of amino acids in proteins. | Some covalent modifications of amino acids in proteins are phosphorylation, acetylation, prenylation, and methylation. |
| 43.List some functions of amino acid derivatives | Amino acid derivatives function as a neurotransmitter, hormones, metabolic activities, immune system, enzymes for chemical reactions, etc. |
| 44. Explain why polypeptides have such variable sequences. | Because there are 20 different amino acids. Even a small polypeptide has an enormous amount of possibilities. |
| 45. What factors limit the size and compositions of polypeptides? | Proteins are limited in size and composition by the efficiency of protein synthesis and by the ability of the polypeptide to fold into a functional structure. |
| 46.Describe the four levels of protein structure. Do all proteins exhibit all four levels? | Not all proteins exhibit all four levels. Hemoglobin for example, does exhibit all four as it is a tetramer of four globin polypeptides. |
| 47. Summarize the features of an α helix and a parallel and antiparallel β sheet. | α helix is right-handed with more than three helical turns The parallel β sheet consists of more than one β pleated sheet running in the same direction connected by right-handed or left-handed crossover connections |
| 48.What properties do fibrous proteins confer on substances such as hair and bones? | Fibrous proteins, which are elongated molecules that often have 1 dominant type of secondary structure, are responsible for the mechanical properties (ex., high tensile strength) of hair, bones, etc. |
| 49. Describe the features of the amino acid sequences that are necessary to form a coiled coil or a left-handed triple helix. | Repetition of amino acid sequences with a certain type of amino acid present in certain positions is necessary to form the protein structures, such as the coiled-coil and triple helix. |
| 50.What distinguishes regular and irregular secondary structures? | The regular secondary structure has similar ϕ and Ψ values in their successive amino acid residues. In contrast, the irregular secondary structures do not have such similarities in ϕ and Ψ values in the successive residues. |
| 51.Explain why knowing a protein’s amino acid sequence is required to determine its tertiary structure. | The interactions between different amino acid residues determine the tertiary structure, which determines the functionality of a protein. |
| 52.Why do turns and loops most often occur on the protein surface? | The loops and turns often occur on the protein surface because of their hydrophilic residues. |
| 53. Which side chains usually occur on a protein’s surface? In its interior? | The polar side chains, mostly the charged polar residues, usually occur on the protein’s surface and the non-polar side chains in its interior |
| 54.Describe some of the common protein structural motifs. | Triple helix motif-This is where three α-helices are further twisted into a single helix Four helix bundle-This is where four α-helices are packed together |
| 55.Why is it useful to compare protein structures in addition to protein sequences? | Evolution tends to conserve the protein structures more than their sequences. Comparing the structure of the proteins and their sequences reveal evolutionary relationships that are not apparent from the sequence only. |
| 56.List the advantages of multiple subunits in proteins. | proteins contain more than one polypeptide chain of subunits. These unite with a specific geometry to give the protein its quaternary structure. Each subunit has its active site.association of subunits provides the structural basis for their functional ac |
| 57.Why can’t proteins have mirror symmetry? | Proteins can not have mirror inversion symmetry because to achieve such symmetries proteins need to have both L- and D- amino acids, which is not the case. |
| 58.Describe the hydropathic index plot for a fIbrous protein such as collagen or keratin | The hydropathic index plot of collagen will mostly shift toward the negative region of the plot. For keratin, every third or fourth residue will show a highly positive shift in the plot. |
| 59. Describe the forces that stabilize proteins, and rank their relative importance. | The forces that stabilize protein structures could be ranked as the 1 hydrophobic effect, 2 electrostatic interactions, 3 disulfide bonds, and 4 metal ion coordination |
| 60.Summarize the results of Anfinsen’s experiment with RNase A. | Anfinsen concluded that the information required to fold a protein into its native, lowest-energy conformation is entirely contained within its sequence of amino acids. |
| 61. Why would it be advantageous for a protein or a segment of a protein to lack defined secondary or tertiary structure | It is advantageous for protein or segment of protein to lack defined secondary or tertiary structure. Those segments are flexible to reduce intracellular crowding and switch between stable conformations depending on cellular conditions or target binding m |
| 62.Describe the structure of myoglobin and haemoglobin. | Hemoglobin is a tetramer composed of four chains of polypeptides with a quaternary structure. Myoglobin is a monomeric protein made of a single polypeptide chain of amino acids with a tertiary structure. |
| 63.Describe the O2 binding behaviour of myoglobin in terms of Po2. | Myoglobin displays a regular curve as you increase the concentration of oxygen, myoglobin becomes saturated very quickly and then levels off. This implies that myoglobin has a high affinity for oxygen |
| 64.Explain the structural basis for cooperative oxygen binding to hemoglobin. | The binding of oxygen by haemoglobin is cooperative ; the protein cannot be considered in terms of four independently oxygen-binding subunits. haemoglobin binds successive oxygens, the oxygen affinity of the subunits increases. The affinity for the fourth |
| 65.Sketch a binding curve (% bound ligand versus ligand concentration )for cooperative and noncooperative binding. | The cooperative binding shows a sigmoidal curve, while the non-cooperative binding shows a logarithmic curve. |
| 66.Explain why the O2 -binding behaviour of myoglobin and haemoglobin can be summed up by single number(p50) | p50 can sum up the behavior of myoglobin and hemoglobin molecules due to the partial pressure of O2 required to bind 50% of the myoglobin molecules. The P 50 of hemoglobin is greater than the P 50 for myoglobin |
| 67.Could a binding protein have a hill constant zero? | NO. It must always have either a negative or a positive one. |
| 68.Describe how myoglobin and haemoglobin function in delivering O2 from the lungs to respiring tissues | From the lung, hemoglobin transports oxygen to the respiring tissue and transfers the oxygen to myoglobin. Then myoglobin facilitates the diffusion of oxygen to the respiring tissues. |
| 69.What is the physiological relevance of the Bohr effect and BPG ? | The Bohr effect states that when CO2 is present, hemoglobin's affinity for oxygen decreases. |
| 70.Explain why mutations can increase or decrease the oxygen affinity and cooperativity of hemoglobin.How can the body compensate for these changes? | Since the structure of hemoglobin is crucial for its usual oxygen binding, a change in the structure of hemoglobin causes the altercation of oxygen binding affinity and the co-operativity of hemoglobin. |
| 1.Define enzyme | Enzymes are proteins that help speed up metabolism, or the chemical reactions in our bodies. They build some substances and break others down. All living things have enzymes. Our bodies naturally produce enzymes. |
| 2.Differentiate between intracellular and extracellular enzymes. | The difference is that intracellular enzymes are produced within the cell and extracellular enzymes are produced outside the cell. |
| 3.What is a coenzyme? | A small organic molecule, acting as a cofactorin a conjugated enzyme, Coenzymes are derived from vitamins or vitamin derivatives. Many vitamins act as coenzymes, esp. B-vitamins. |
| 4. What are apoenzymes? | Apoenzyme is an enzymatically inactive protein part of an enzyme, which requires a cofactor for its activity. Apart from catalytic RNA, most of the enzymes are proteins. Enzymes that do not require any cofactor are known as simple enzymes, e.g. pepsin, tr |
| 5.Discuss the classification of enzymes. | Oxidoreductases,Transferases,Hydrolases,Lyases,Ligases,Isomerases |
| 6. Describe in brief the different factors affecting enzyme actions | Enzyme activity can be affected by a variety of factors, such as temperature, pH, and concentration. Enzymes work best within specific temperature and pH ranges, and sub-optimal conditions can cause an enzyme to lose its ability to bind to a substrate. |
| 7.Define the Michaleis Menton equation . The effect of enzyme concentration and substrate concentration. | the enzyme reversibly combines with its substrate to form an ES complex that subsequently breaks down to product, regenerating the free enzyme. |
| 8.Describe the actions of Inhibiting agents. | substance that slows down or stops the normal catalytic function of an enzyme by binding to the enzyme.substance that can diminish velocity of an enzyme-catalyzed reaction is called inhibitor.Inhibitors are chemicals that reduce rate of enzymatic reaction |
| 9. What are Irreversible inhibitions? | An irreversible inhibitorinactivates an enzyme by binding to its active site by a strong covalent bond. Permanently deactivates the enzyme. Irreversible inhibitors do not resemble substrates. |
| 10.What are Reversible Inhibitions? | Reversible inhibitor is one that, once removed, allows the enzyme it was inhibiting to begin working again. |
| 11.Define Competitive inhibition. | occurs when the inhibitor binds reversibly to the same site that the substrate would normally occupy and, therefore, competes with the substrate for that site. |
| 12. Define Non-competitive inhibition. | not influenced by the concentration of the substrate. It inhibits by binding irreversibly to the enzyme but not at the active site. A non-competitive inhibitor decreases enzyme activity by binding to a site on the enzyme other than the active site. |
| 13.What are Cofactors? | non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst (a catalyst is a substance that increases the rate of a chemical reaction). |
| 14.What are Allosteric enzymes? | Allosteric enzymes are enzymes which have an additional site, as well as the active site They are unique in that they have the ability to respond to multiple different conditions . |
| 15.Describe the Template or Lock and Key model of enzyme action | Lock-and-key model is a model for enzyme-substrate interaction suggesting that the enzyme and the substrate possess specific complementary geometric shapes that fit exactly into one another. |
| 16. Describe the induced fit model of enzyme action | The induced-fit model states a substrate binds to an active site and both change shape slightly, creating an ideal fit for catalysis. |
| 17. What are Isoenzymes | enzymes that catalyze the same reaction but differ in their physical properties because of genetically determined differences in amino acid sequence. Isoenzymes may contain different numbers of charged amino acids and be separated from each other by elect |
| 18.Write a note on the regulation on enzyme activity | Enzymes can be regulated by other molecules that either increase or reduce their activity. Molecules that increase the activity of an enzyme are called activators, while molecules that decrease the activity of an enzyme are called inhibitors. |
| 19. What are Coenzymes? | defined as an organic molecule that binds to the active sites of certain enzymes to assist in the catalysis of a reaction.coenzymes can function as intermediate carriers of electrons |
| 20.Mention the important functions of coenzymes | Coenzymes can function as intermediate carriers of electrons during these reactions or be transferred between enzymes as functional groups. |
| 21.Enzyme in clinical diagnosis. | Relatively small group of enzymes are actively secreted into the plasma by certain organs. Large number of enzyme species are released from cells during normal cell turnover. |
| 22.What is the relationship between cofactors, coenzymes, cosubstrates, and prosthetic groups? | They all bind tightly or loosely to proteins or enzymes and help them function. Cofactor is a specific type of coenzyme. |
| 23. What is the function of an enzyme in a chemical reaction? | Enzymes speed up chemical reactions by lowering the amount of activation energy needed for the reaction to happen. |
| 24.What happens to the enzymes when the body temperature rises from 37ᵒC to 42ᵒC? | Extreme high temperatures can cause an enzyme to lose its shape (denature) and stop working. pH: Each enzyme has an optimum pH range. |
| 25.If an enzyme has broken down and is non-functional,what would happen to the chemical reaction normally facilitated by the enzyme? Explain. | Normally enzymes reduce the activation energy needed to start these reactions; without them, most such reactions would not take place at a useful rate. |
| 26.Why is an enzymes active site important to the function of the enzyme? | The active site of the enzyme is what attaches to the substrate and what changes the substrate's structure, making it more reactive |
| 27.Why is the enzymes regulatory binding site important for controlling the activity of the enzyme? | enzymes guide and regulate the metabolism of a cell, they tend to be carefully controlled. All enzymes should not be activated at the same time or in the same cell; |
| 28.Why are coenzymes (derived from vitamins) important to the function of some enzymes? | coenzyme is defined as an organic molecule that binds to the active sites of certain enzymes to assist in the catalysis of a reaction. |
| 29.What properties distinguish enzymes from other catalysts? | The properties that distinguish enzymes from other catalysts are condition of reaction, the rate of reaction, control of reaction, and reaction specificity. |
| 1.What are vitamins? | Vitamins are organic compounds required by the body in trace amounts to perform specific cellular functions. |
| 2.Write in brief the classification of vitamins. | fat and water soluble |
| 3.Give an account of Vitamin A. Occurrence,biochemical functions,physiological functions,deficiency. | fat soluble preformed vit A - animal products pro vit A - plant based, orange/yellow eg carrots and pumpkin too much vit A - causes birth defects too little vit A - more prone to infectious diseases |
| 4.Briefly write a note on Vitamin D. Occurrence,biochemical functions,physiological functions,deficiency | fat soluble found in flesh of fatty fish (salmon, tuna), red meat and liver too much vit D - hypercalcemia too little vit D - rickets, osteoporosis, osteomalacia, |
| 5.Write a note on Vitamin E (Tocopherols). Occurrence,biochemical functions,physiological functions,deficiency | fat soluble found in sunflower seeds, almonds, peanuts, green beans bell peppers too much vit E - high risk of bleeding, muscle weakness, fatigue, nausea, diarrhoea too little vit E - nerve and muscle damage, loss of control of movement |
| 6.Write a note on Vitamin K . Occurrence,biochemical functions,physiological functions,deficiency | fat soluble found in leafy greens: kale, spinach, broccoli, brussel sprouts, cabbage, lettuce helps make proteins for blood clotting, building of healthy bones too much vit K - jaundice, too little vit K - haemorrhaging |
| 7.Write a note on Vitamin C. Occurrence,biochemical functions,physiological functions,deficiency | water soluble found in citrus, tomatoes potatoes kiwis broccoli too much vit C - nausea, vomiting, diarrhea and stomach cramps too little vit C - scurvy |
| 8. List different members of Vitamin B – Complex. | thiamine B1 riboflavin B 2 niacin B3 pantothenic acid B5 Pyridoxine B6 biotin B7 Folic acid B9 Cobalamin B12 |
| 9. Write a note on Thiamine (Vitamin B1). . Occurrence,biochemical functions,physiological functions,deficiency | water soluble found in bread, cereal, pork, fish, beans, lentils too much thiamine - the body will absorb less and flush out the rest in urine too little thiamine - fatigue, loss of appetite, muscle weakness |
| 10. Write occurrence, sources, functions and deficiency symptoms of Riboflavin (Vitamin B2). | water soluble found in milk, cheese, yoghurt, eggs, lean beef and pork, liver, salmon Too much vit B2 - excess is urinated Too little vit B2 - fatigue, swollen throat, |
| 11.Write occurrence, sources, functions and deficiency symptoms of Niacin or Vitamin B3 | Niacin or Vitamin B3 is a water-soluble vitamin found in foods such as fish, meat, poultry, and whole grains. It is involved in energy metabolism, DNA repair.Deficiency in niacin leads to pellagra |
| 12.Write occurrence, sources, functions and deficiency symptoms of Pyridoxine or Vitamin B6 | Pyridoxine or Vitamin B6 is a water-soluble vitamin found in foods such as meats, fish, and starchy vegetables. It plays a role in protein metabolism, Deficiency in pyridoxine can lead to anemia |
| 13.Write occurrence, sources, functions and deficiency symptoms of Pantothenic acid or Vitamin B5 | Pantothenic acid or Vitamin B5 is a water-soluble vitamin that is widely distributed in food, especially in whole grains, legumes, and eggs. It plays a role in the synthesis of coenzyme |
| 14.Write a note on Vitamin B12. Occurrence,biochemical functions,physiological functions,deficiency | Vitamin B12 is a water-soluble vitamin that is found in foods of animal origin such as meat, fish, and dairy products. It plays an important role in the formation of red blood cells Deficiency in vitamin B12 leads to pernicious anemia |
| 15.What are Folic Acids? Give an account of them Occurrence,biochemical functions,physiological functions,deficiency | Folic acid is a water-soluble B vitamin that is found in leafy green vegetables, fruits, and fortified grains. It plays an important role in the formation of red blood cells Deficiency in folic acid can lead to megaloblastic anemia |
| 16.Write a note on Biotin. Occurrence,biochemical functions,physiological functions,deficiency | Biotin is a water-soluble B vitamin that is found in small amounts in a variety of foods such as eggs, nuts, and dairy products. It plays a role in the metabolism |
| 17. What are Lipoic acid? Occurrence,biochemical functions,physiological functions,deficiency | Lipoic acid is a compound that is related to B-vitamins and is found in small amounts in foods such as spinach, broccoli, and yeast. . Deficiency in lipoic acid is rare, but symptoms can include fatigue, |
| 18.Give an account of Inositol | Inositol is a carbohydrate that belongs to the B-vitamin family, it is found in small amounts in foods such as whole grains, nuts, and seeds. It plays a role in maintaining healthy cell membranes |
| 19.Write short notes on . Beri–Beri,Pellagra, ostomalacia ,pernicious anemia,rickets, Scurvy | Beri-beri is a disease caused by deficiency in thiamine (vitamin B1) characterized by symptoms such as muscle weakness, fatigue, and nerve damage. Pellagra is a disease caused by deficiency in niacin |
| 20.What are Vitamin P? | bioflavonoids, |
| 21. What is Coenzyme Q ? | Coenzyme Q, also known as ubiquinone, is a compound that plays an important role in the production of energy within cells |
| 1.Structure of purine and pyrimidine nucleotides. | both purine and pyrimidine are heterocyclic compounds |
| What are nucleotides? | organic molecules consisting of a: nucleoside and a phosphate (an anion (negative ion) consisting of a phosphate and 4 oxygens [PO43-]) |
| 2.Proprietes of nucleotides. | nucleotides are components of some of the central cofactors of metabolism all cells can synthesize nucleotides |
| 3.Nucleotides in metabolism(examples). | .Nucleotides in metabolism(examples). (FAD (flavin adenine dinucleotide), NAD+ (Nicotinamide adenine dinucleotide) and coenzyme A |
Created by:
111277361734879
Popular Chemistry sets