Protein Chemistry Bsc Nursing & Bpt


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useful for BSC nursing and BPT 1st year students. Covers the topics as per syllabus recommended by baba farid university of health sciences.

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Protein Chemistry Bsc Nursing & Bpt

  1. 1. Proteins Shiv Ram krishn Senior Demonstrator, Biochemistry, GSMCH.
  2. 2. Syllabus <ul><li>Definition </li></ul><ul><li>Sources </li></ul><ul><li>Classification </li></ul><ul><li>Simple Proteins </li></ul><ul><li>Conjugated proteins </li></ul><ul><li>Derived Proteins </li></ul><ul><li>Properties </li></ul>
  3. 3. Introduction <ul><li>Dr. Harpreet  Amino acid Chemistry </li></ul><ul><li>Amino acid definition </li></ul><ul><li>Structure </li></ul><ul><li>Classification  Structural </li></ul><ul><li> Nutritional </li></ul><ul><li> Functional </li></ul><ul><li>Importance </li></ul><ul><li>Properties  Isoelectric pH </li></ul><ul><li>How amino acids Polymerize to form Proteins? </li></ul>
  4. 4. Definition Of Proteins <ul><li>Term Protein  Berzelius  From Greek Word Proteios meaning: Holding First Place or pre eminent. </li></ul><ul><li>Most abundant organic molecules of living system. </li></ul><ul><li>C= 50-55% </li></ul><ul><li>H= 6-7.3% </li></ul><ul><li>O= 19-24% </li></ul><ul><li>N= 13-19% </li></ul><ul><li>S= 0-4% </li></ul><ul><li>P, Fe, Cu, I, Mg, Mn, Zn </li></ul>
  5. 5. <ul><li>Present in each & every cell.(50% cellular dry weight) </li></ul><ul><li>Form fundamental basis of structure & function of life. </li></ul><ul><li>Have High Molecular weight.(5000-25,00,000) </li></ul><ul><li>Nitrogenous macromolecules composed of many amino acids  Unbranched polymers of L- α -aminoacids. </li></ul><ul><li>20 standard amino acids in different sequence & different number combine to form indefinite no. of proteins. </li></ul>
  6. 6. How amino acids combine to form protein
  7. 7. Functions of Proteins <ul><li>Sole source to replace Nitrogen of the body. </li></ul><ul><li>Enzymes  Biochemical catalyst </li></ul><ul><li>Immunoglobulins  IgG, IgA, IgM, IgD, IgE  body defence </li></ul><ul><li>Several Hormones  Insulin, Oxytocin </li></ul><ul><li>Receptors </li></ul><ul><li>Transport Proteins  Albumin </li></ul><ul><li>Storage Proteins  Ferritin </li></ul><ul><li>Respiratory Pigment, ETC  cytochromes, Hemoglobin, Myoglobin </li></ul><ul><li>Exert Osmotic Pressure  Electrolyte & water balance </li></ul><ul><li>Blood Clotting Factors  Fibrinogen, Thrombin, Prothrombin </li></ul><ul><li>Provide Energy during prolonged starvation. </li></ul><ul><li>Associated with structure & strength of body. </li></ul><ul><ul><li>Collagen, Elastin  Bone matrix, Vascular system </li></ul></ul><ul><ul><li>Α -keratin  epidermal tissues </li></ul></ul><ul><ul><li>Actin, Myosin  Muscle fibre(Contractile proteins) </li></ul></ul>
  8. 8. Sources of proteins <ul><li>Animal Sources </li></ul><ul><ul><li>Egg </li></ul></ul><ul><ul><li>Milk </li></ul></ul><ul><ul><li>Fish </li></ul></ul><ul><ul><li>Meat </li></ul></ul><ul><ul><ul><li>Pork </li></ul></ul></ul><ul><ul><ul><li>Beef </li></ul></ul></ul><ul><ul><ul><li>Mutton </li></ul></ul></ul><ul><ul><ul><li>chicken </li></ul></ul></ul><ul><ul><li>Liver </li></ul></ul><ul><li>Plant sources </li></ul><ul><ul><li>Cereals </li></ul></ul><ul><ul><ul><li>Wheat </li></ul></ul></ul><ul><ul><ul><li>Rice </li></ul></ul></ul><ul><ul><ul><li>Maize </li></ul></ul></ul><ul><ul><ul><li>Barley </li></ul></ul></ul><ul><ul><li>Legumes </li></ul></ul><ul><ul><li>Pulses </li></ul></ul><ul><ul><ul><li>Red gram </li></ul></ul></ul><ul><ul><ul><li>Bengal gram </li></ul></ul></ul><ul><ul><ul><li>Green gram </li></ul></ul></ul><ul><ul><ul><li>Peas </li></ul></ul></ul><ul><ul><ul><li>Soyabean </li></ul></ul></ul><ul><ul><li>Cashew nut </li></ul></ul><ul><ul><li>Ground nut </li></ul></ul><ul><ul><li>Roots &Tubers </li></ul></ul>
  9. 9. Definition in short <ul><li>Proteins are high molecular weight, nitrogenous, organic macromolecules present in each & every cell of living system forming the fundamental basis of structure and function of life. </li></ul>
  10. 10. Questions <ul><li>Define Proteins. </li></ul><ul><li>Give the chemical constitution of proteins. </li></ul><ul><li>Explain the formation of proteins. How? </li></ul><ul><li>Who coined the term protein? </li></ul><ul><li>Where are proteins found? </li></ul><ul><li>What does the term protein means? </li></ul><ul><li>Give some examples showing structural role of proteins. </li></ul><ul><li>Give some examples showing dynamic functions of proteins. </li></ul><ul><li>Name some vegetable sources of proteins. </li></ul><ul><li>Name some animal sources of proteins. </li></ul>
  11. 11. Any Doubts <ul><li>Insulin function </li></ul><ul><li>Glucagon function </li></ul><ul><li>None other question asked. </li></ul>
  12. 12. Thanks
  13. 13. Classification of Proteins Shape & Size Functional Properties Solubility & Physical Properties Fibrous Globular Defence proteins Contractile Proteins Hormones Enzymes Structural proteins Respiratory Proteins Simple Proteins Conjugated Proteins Derived Proteins Protamines Scleroproteins Glutelins Gliadins (Prolamines) Globulins Albumins Histones Nucleo proteins Metallo proteins Lipoproteins Phospho proteins Chromo proteins Glycoproteins Muco Proteins Primary derived Secondary derived Proteans Coagulated proteins Metaproteins Proteoses peptides Peptones
  14. 14. Simple Proteins Basic Protein, N.A. + Histone=Nucleoprotein, Porphyrin+Histone=conjugated Protein, Repressor of template activity of DNA in synthesis of RNA’ Hemoglobin  Globin  Histone  His & lys rich Alkaline Arginine, Histidine _ NH3 Water, Dil. Acid, Salt solution Histones Salmine Sardine Cyprinine(of fish sperms & testes) Basic protein, N.A+protamine=Nucleoprotein 7.4 Cysteine Tryptophan tyrosine Arginine rich _ Water Dilute acid Dilute alkali Dilute NH3 small Protamine Eg. Use pI AA- AA+ Heat coagulability Insolubility Solubility Size & shape Protein type
  15. 15. Simple proteins contd. Rice  Oryzein, Wheat  Glutelin Glutamic acid rich + Water, Neutral salt solution Dilute acid, Dilute alkali Large molecules Glutelins Wheat-  Gliadin, Barley  Hordein Plant Protein Lysine Proline Water, Salt soln., Absolute alcohol Alcohol(50-80% C2H5OH) Gliadin (Prolamines) Heme+globulin=Hemopexin, Heme+metal=Transferrin, Ceruloplasmin, Heme+Carbohydrate=Immunoglobulin, Eggs  Ovoglobulin Milk  Lactoglobulin Legumes  Legumin Precipitated by half saturation with ammonium sulfate or full saturation with sodium chloride. + water Dilute neutral salt solutions Globulins Legumes—legumelin, Cereals—Leucosin, Egg—Ovalbumin Milk--Lactalbumin Precipitated out of solution by saturation by ammonium sulfate. 4.7 Glycine Cagulable by heat  Product  insoluble in water & dil. Salt solution Water, Dilute salt solution Albumin
  16. 16. Simple proteins contd. scleroproteins Found in Connective tissue, In Yellow elastic fibres, In ligament, tendon Formed in large amount during pregnancy Elastin is hydrolyzed by pancreatic elastase Cysteine, Methionine, 5-Hydroxylysine, Histidine Alanine, Leucine, Valine, Proline Elastins Found in connective tissue,Bone Collagen  Tannic acid  tough, hard, Collagen  boiling  gelatin  highly soluble, easily digestible  cool  gel  no tryptophan Insoluble in all neutral salt solvents Long, thin, partially crystalline Collagen Present in chidermal tissuesuch as horn, hair, nails, wool, hoofs, feathers(supporting structures) spider’s web, silk, reptilian scales Cysteine absent Hard keratin  His:Lys:Arg  1:4:12, Soft or pseudokeratins  A.A. not in same ratio, Neurokeratins  1:2:2, Human Hair  alpha keratin  cysteine rich, Beta Keratin  Glycine, Alanine rich low Fibrous Keratins
  17. 17. Conjugated Proteins <ul><li>Conjugated Protein= Simple Protein + Prosthetic Group(non Protein group) </li></ul><ul><li>Holoprotein= Apoprotein + Prosthetic group </li></ul><ul><ul><li>Nucleoproteins = Protamine/ Histone + Nucleic acid </li></ul></ul><ul><ul><ul><li>Deoxyribonucleoproteins: DNA as prosthetic group. Found in Nuclei, Mitochondria, Chloroplasts. </li></ul></ul></ul><ul><ul><ul><li>Ribonucleoproteins: RNA as prosthetic group. Found in Nucleoli, ribosome granules. </li></ul></ul></ul><ul><ul><li>Nucleoproteins are found in: </li></ul></ul><ul><ul><ul><li>Cell Nuclei. </li></ul></ul></ul><ul><ul><ul><li>As constituent of chromatin </li></ul></ul></ul><ul><ul><ul><li>Abundant in yeast, Asparagus tip in plants, thymus, glandular organs, sperms. </li></ul></ul></ul>
  18. 18. Conjugated proteins contd. <ul><li>Mucoproteins or mucoids: </li></ul><ul><li>Simple Proteins + Mucopolysaccharides(hyaluronic acid, chondroitin sulphate containing >4% N-acetylated hexosamine, uronic acid, sialic acid). </li></ul><ul><li>Examples: Mucoproteins found in/as </li></ul><ul><ul><li>α -ovomucoid & β -ovomucoid of eggwhite. </li></ul></ul><ul><ul><li>Mucins </li></ul></ul><ul><ul><li>Blood group substances </li></ul></ul><ul><ul><li>FSH, LH, HCG </li></ul></ul><ul><ul><li>Vitreous humor </li></ul></ul><ul><ul><li>Submaxillary gland </li></ul></ul><ul><ul><li>Umbilical cord(mucoproteins present in large amount) </li></ul></ul>
  19. 19. Conjugated proteins contd. <ul><li>Glycoproteins= Simple Protein + Carbohydrate moiety(<4% mannose, galactose, fucose, xylose, arabinose in oligosaccharide chains). </li></ul><ul><li>Examples: </li></ul><ul><ul><li>Mucins </li></ul></ul><ul><ul><li>Immunoglobulins </li></ul></ul><ul><ul><li>Complements </li></ul></ul><ul><ul><li>Many enzymes </li></ul></ul>
  20. 20. Conjugated proteins contd. <ul><li>Chromoproteins= simple protein + coloured substances. </li></ul><ul><li>Hemoproteins = simple protein + Heme(red colour) </li></ul><ul><ul><li>Hemoglobin  in RBC </li></ul></ul><ul><ul><li>Cytochromes  Respiratory chains </li></ul></ul><ul><ul><li>Catalase  H 2 O 2 -------  H2O + O2 </li></ul></ul><ul><ul><li>Peroxidase  oxidative enzyme </li></ul></ul><ul><li>Flavoproteins = simple protein + Riboflavin(yellow colour)  it is cellular oxidation reduction protein. </li></ul><ul><li>Visual purple =Simple protein + Carotenoid pigment (Purple)  Found in retina </li></ul>
  21. 21. Conjugated proteins continued. <ul><li>Phosphoproteins = simple protein + phosphoric acid as organic phosphate </li></ul><ul><ul><li>Milk  casein </li></ul></ul><ul><ul><li>Egg yolk  ovovitellin </li></ul></ul><ul><li>Lipoproteins = simple proteins + Lipids </li></ul><ul><ul><li>HDL, VLDL, LDL, Chylomicrons. </li></ul></ul><ul><li>Metalloproteins = Simple protein + Metal ions(Fe, Co, Mn, Zn, Cu, Mg) </li></ul><ul><ul><li>Ferritin  Fe </li></ul></ul><ul><ul><li>Ceruloplasmin  Cu </li></ul></ul><ul><ul><li>Carbonic anhydrase  Zn </li></ul></ul>
  22. 22. Derived proteins <ul><li>Simple & conjugated proteins Physical & chemical factors  protein products (derived proteins) </li></ul><ul><li>Derived proteins are of 2 types: </li></ul><ul><ul><li>Primary derived proteins </li></ul></ul><ul><ul><li>Secondary derived proteins </li></ul></ul>
  23. 23. Primary derived proteins <ul><li>These are denatured or coagulated proteins. </li></ul><ul><li>Molecular weight is same as native protein. </li></ul><ul><li>Differ in solubility, precipitation & crystallization. </li></ul><ul><li>Physical & chemical factors involved are  Heat, X-rays, UV rays, vigorous shaking, acids, alkalies. </li></ul><ul><li>There is intramolecular rearrangement,although peptide bonds remain intact. </li></ul><ul><li>Proteans: </li></ul><ul><ul><li>Insoluble products formed by action of water, very dilute acids & enzymes. </li></ul></ul><ul><ul><ul><li>Eg. Myosan from myosin </li></ul></ul></ul><ul><ul><ul><li>Edestan from Elastin </li></ul></ul></ul><ul><ul><ul><li>Fibrin from Fibrinogen </li></ul></ul></ul><ul><li>Metaproteins: </li></ul><ul><ul><li>Proteans--  acid & alkalies-  metaproteins. </li></ul></ul><ul><ul><li>Soluble in dilute acids & alkalies. </li></ul></ul><ul><ul><li>Insoluble in neutral solvents. </li></ul></ul><ul><ul><ul><li>Eg. Acid & alkali metaproteins. </li></ul></ul></ul><ul><li>Coagulated proteins: </li></ul><ul><ul><li>Native protein---  Heat, alcohol--  coagulated protein(insoluble product) </li></ul></ul><ul><ul><ul><li>Eg.: cooked meat, cooked egg albumin. </li></ul></ul></ul>
  24. 24. Secondary derived proteins <ul><li>Formed by progressive hydrolysis of proteins at their peptide linkages. </li></ul>Proteins Proteoses (Water soluble, Heat coagulable, pptd. By ammonium sulphate) Peptones (water soluble, Not heat coagulable, Not pptd. By ammonium sulphate, pptd. By phosphotugustic acid.) Peptides (Water soluble, Not heat coagulable, Not pptd. By ammonium sulphate Pptd. By phosphotungustic acid)
  25. 25. Complete hydrolysis of protein <ul><li>Protein  Protean  Meta protein  Proteose  Peptone  Peptide  Aminoacid </li></ul>
  26. 26. General properties of proteins <ul><li>Taste: Tasteless. Hydrolytic products are bitter. </li></ul><ul><li>Odour: Odourless. </li></ul><ul><ul><li>Protein heated to dryness-  brown colour  odour of burning feather. </li></ul></ul><ul><li>Molecular weight: High molecular weight(macromolecules). </li></ul><ul><ul><li>S. Albumin= 69000 </li></ul></ul><ul><ul><li>S. Globulin= 176,000 </li></ul></ul><ul><ul><li>Fibrinogen= 330,000 </li></ul></ul><ul><ul><li>Hemoglobin= 67,000 </li></ul></ul><ul><ul><li>Cytochrome C= 15,600 </li></ul></ul><ul><ul><li>Pepsin= 35,500 </li></ul></ul><ul><ul><li>Catalase= 250,000 </li></ul></ul><ul><li>Viscosity: Long molecules(fibrous) more viscous than globular proteins. Eg. Fibrinogen more viscous than albumin. </li></ul><ul><li>Hydration: Amino(-NH2), and carboxyl(-COOH) group are easily hydrated. </li></ul><ul><li>Amphoteric nature: </li></ul><ul><li>Protein molecule  -NH2 group as well as –COOH group present  these ionize & act as proton donor or acceptor  thus protein act as acid and base both  Ampholyte  at pI it act as a dipolar ion  zwitter ion or hybrid ion  net charge at pI =0. </li></ul>
  27. 27. General properties contd. <ul><li>Heat coagulation: maximum coagulation take place at pI. Proteins get denatured. </li></ul><ul><li>8. <----------------------------------------pI--------------------------------------------  </li></ul><ul><li> acidic alkaline </li></ul><ul><li> </li></ul><ul><li> Protein becomes Protein becomes </li></ul><ul><li>cation by accepting proton anion by donating proton </li></ul><ul><li> migrate towards anode migrate towards cathode </li></ul><ul><li>This property is used for separation of proteins by electrophoresis. </li></ul>
  28. 28. General properties contd. <ul><li>9. Precipitation: </li></ul><ul><ul><li>Proteins can be pptd. By some +ve or –ve ions. </li></ul></ul><ul><ul><li>this is used for isolation of proteins. </li></ul></ul><ul><ul><li>in deproteinization of blood & biological fluids for analysis. </li></ul></ul><ul><ul><li>in preparation of protein derivatives. </li></ul></ul><ul><ul><li>+ve ions used are: Zn+2, Ca+2, Hg+2, Fe+3, Cu+2, Pb+2 </li></ul></ul><ul><ul><li>-ve ions used are: Tungstic acid, phosphotungstic acid, trichloroacetic acid, picric acid, tannic acid, ferrocyanic acid, sulphosalicylic acid. </li></ul></ul>
  29. 29. General properties contd. <ul><li>10. Colour reactions of proteins: </li></ul>α -Amino acid Blue colour Ninhydrin reaction Histidine & 2 or more peptide linkage Purple violet Biuret reaction Sulphur containing AA Black colour Lead acetate test Cysteine, cystine Red colour Sullivan reaction Cysteine Reddish colour Nitroprusside reaction Tryptophan Hopkins Cole reaction Arginine Red colour Sakaguchi test tyrosine Pink red Millon’s test Phenylalanine, tyrosine,tryptophan Yellow to orange Xanthoproteic reaction Aminoacid involved Colour developed Name of Reaction