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Proteins- structure & properties.
- 1. Proteins…. -Peptide linkage -Stucture of proteins -Some properties Hii…………..
- 2. PEPTIDE LINKAGE Amino acid + amino acid amide -H2O O H C N A link between -C=O group Of 1 amino acid & -NH Group of other amino acid T think I am the strongest since I hav a lot of proteins
- 3. Dipeptide bond Ala trp Surprise……….surprise!!!! Are you ready!!!!!!!
- 4. tripeptide Ala trp pro Hey…Smile beuties…..
- 5. tetrapeptide cys leu tyr ala Friendship should be like this yaaar….
- 7. POLYPEPTIDE The strongest of all….
- 9. Franz hofmiester -German scientist & physician -Observed biuret reactions in proteins -proteins-linear chains of alpha amino acids-1902 -Peptide model -amide linkage Emil fischer Hats off to them………
- 10. PRIMARY STRUCTURE The order in which the amino acids are attached by peptide linkage. Starts from N-terminal end to the C-terminal end.
- 11. The primary structure also requires specifying he cross-linking atoms, specifying the cysteines nvolved in the protein's disulfide bonds. Lets see in detail…
- 12. What doesprimary structuretell us?? sequence number composition kind rder how many which one acidic basic neutral polar/non-pola See the uses….
- 13. Determination of amino acid composition Lets discover somthing
- 14. proteins Hydrolyse peptide bonds Seperated amino acids Individual Amino acids colour extracted Amino acid Composition determined 6N,HCl 110 C ,24hrs chromatography Ninhydrin test solvent
- 15. Advantage- Amino acid composition & kind can be determined Disadvantage- Sequence cannot be determined Aey……………. Ayyoooooooooo…….
- 16. Determination of sequence of amino acids End amino acid full sequence (atleast) Sanger dansyl EDMANs degradation method chloride Hey…one more thing
- 17. -introduced SANGER method -1953 -Sequenced insulin -specific cleavage of protein & polypeptides Frederick sanger Well done sir……..
- 18. Sangers method/FDNB Method Frederick Sanger -1953 + N-terminal of dinitrophenyl amino acid derivative(yellow) End terminal Amino acid
- 19. Dansyl chloride + N-terminal of amino acid Sulphonamide derivative complex End terminal Amino acid formed Its easy I think…..
- 20. EDMANs degradation Divide & conqure First round Second round First round 21 3 4 1 2 3 4 3 41 2+ + henyliso- peptide phenylthiocarbomyl derivative iocynate Peptide shortened By 1 residue labelling release e process repeats till the full sequence is determined. Very imp..
- 21. Kaj Ulrik Linderstrøm -Introduced primary structure of protein -in Stanford in 1953 -he was elected as a Foreign Member of the Royal Society (ForMemRS) We miss u sir…..
- 22. SECONDARY STRUCTURE oiling of the polypeptide chains through HYDROGEN BONDS. Alpha helix beta-pleated sheet
- 23. pha-helix iling of the polypeptide chain so that the amino acids which are 4 positions apart are brought closer through hydrogen bonds. =O group of amino acid -NH group of 4rth amino ac istance between –adjacent amino acids – 1.5A - one turn – 5.4A HYDROGEN BONDED
- 24. Wooow I love those curly hairs!! air is made up of a protein alled keratin, hich forms a helical shape. his protein has sulfur bonds, nd the more sulfur links it has, he curlier a person’s hair will be. Lovely butterfly….
- 25. eta-pleated sheet hen 2 polypeptide chains or 2 separate regions in the same hains lie side by side that are connected by hydrogen bonds.
- 27. Difference Alpha-helix beta pleated sheet 1.Rod like 2.Helical / coiled 3.Common 4.Adjacent amino acds-1.5A 1.Sheet like 2.Fully extended 3.Less common 4.Adjacent amino acids-3.5A Only 4 differences…???.
- 28. Tertiary structure Folding & refolding of the polypeptide chain to bring the amino acids closer that are far apart.
- 29. Eg 1.Myoglobin -extremely compact -has 53 amino acid residues -75% ,8 helical regions -25%,non helical regions(proline) -interior-nonpolar AA -exterior-polar & nonpolar AA CHARACTERISTICS -No disulphide bonds -contains heme
- 30. In humans,myoglobin is only found in the bloodstream after muscle injury. It is an abnormal finding, and can be diagnostically relevant when found in blood. [2]
- 31. Eg2. Ribonuclease -duck /kidney shaped -has 124 amino acids -4 disulphide bonds between 8 AA 26 40 58 65 S S S S S S S S 84 95 110 72 -NH end-lysine -COO end-valine
- 32. Oh my god!!!! It is first line defence against RNA virus ts acts in RNA interference/post transcriptional gene silencing.
- 33. QUARTERNARY STRUCTURE lding of multiple polypeptide chains ,ie-protein-protein interac Eg.haemoglobin – consists of 4 subunits - 2 alpha-2 haem parts - 2 beta -2 haem parts
- 34. Properties of proteins 1.AMPHOTERIC NATURE acids bases -ISOELECTRIC POINT (pI) +ve charges = -ve charges -net charge =0 -solubility,osmotic pressure,viscosity = minimum Ok….lets concentrate
- 35. 2.DENATURATION -Lose of proteins biological activity due some external stress. Physical organic solvents heavy metals -cooling -freezing -rubbing -agitation -heat -radiation -ethanol -isopropanol -Hg 2+ -Ag+ -Pb+ Wat to do now??
- 36. HOW DENATURATION OCCURS AT DIFFERENT LEVELS 1.QUARTERNARY Dissociation of protein subunits 2.TERTIARY breakage of interactions Covalent dipole-dipole vander-waals 3.SECONDARY Dissociation of alpha helix & beta pleated sheet ATTENSION- primary structure is the powerful one……. Wat happened To my proteins??
- 39. SO SAD KNO!!!!!! Cataracts are caused by the denaturation of proteins in the lenses of the eyes.
- 40. RENATURATION-REVERSIBLE Every action has an equal & opp reaction
- 41. Knowing about proteins was interesting for me… Hope for u all tooo…. Thnx……..