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Proteins 1. 2. 3. 4. 5. 6. 7. 8. 9. 10. 11. 12. 13. 14. 15. 16. 17. 18. 19. 20. 21. 22. 23. 24. 25. 26. 27. 28. 29. 30. 31. 32. 33. 34. 35. 36. 37. Aminoacids are called as Magic 20 because they form the basic components of life Amino acids are Mono or Di carboxylic acids with one or two amino groups (NH2). Essential amino acids cannot be synthesized in the body Essential amino acids are 1 to 8 in adults and 1 to 10 in children The 10 essential amino acids are, Valine, Leucine, Isoleucine, Phenylalanine, Tryptophan,Methionine,Lysine,Threonine,Arginine and Histidine. Easy way to remember 7 essential amino acids is the code HIT LAMP – Histidine, Isoleucine, Tryptophan, Lysine, Arginine, Methione, Phenylalanine Non essential amino acids can be synthesized in the body The 10 non essential amino acids are Alanine, Serine, Proline, Glutamic acid, Aspartic acid, Tyrosine, Cysteine, Asparagine, Glutamine and Glycine. Easy way to remember non essential amino acids is the codes ACT – Alanine-Cysteine-Tyrosine, GAP – Glutamic acid-Aspartic acid- Proline, GAS – Glycine-Asparagine-Serine Non protein forms of amino acids are Ornithine, Citrulline, Cystine and Methionine. Easy way to remember Non protein amino acids is the code MOC – Methionine-Ornithine-Citrulline Sulphur containing amino acids – Methionine, Cysteine, Cystine Simplest amino acid- Glycine. No assymetryic carbon atom present Derived amino acid – Cystine. Formed from other amino acids by enzymatic reaction Alkaline amino acids having Alkyl side chains- Glycine, Alanine, Valine, Leucine, Isoleucine Aromatic amino acid – Phenyl alanine, Tyrosine, Tryptophan Basic amino acid – R group contains nitrogen atom- Lysine, Arginine Dibasic amino acids- Lysine, Arginine, Histidine Acidic amino acids- R group contains carboxyl acid Isoelectric pH- pH at which amino acid becomes neutral in Zwitter ion form. Symbol is pI. Polypeptide is the Primary structure of protein Secondary structure- local 3D folding of polypeptides by covalent bonds- Alpha helix, Beta pleated sheet Tertiary structure- Further folding of secondary structure- Myoglobin Native conformation- Natural conformation by unique arrangement of amino acids Structural Motifs- Peculiar combination of secondary structure of proteins Chaperones- Heat shock proteins. Synthesized when the temperature rises Salt linkage-Electrostatic or Ionic linkages found in Proteins Protein data book- Structure of various Proteins is studied using X ray diffraction and stored in data base Methods to separate proteins- Electrophoresis, Chromatography, HPLC, Affinity chromatography London dispersion and Vander Waal forces- Weakest of non covalent bonds Beta pleated structure- Beta helix structure of proteins Alpha helix- Formed by hydrogen bonding between C=O and N-H groups of peptide bonds Forces of proteins- Hydrogen bond, Ionic bond, Covalent bond, Hydrophobic bond NMR- Nuclear Magnetic Resonance. Used to study protein structure M-Protein- Antiphagocytic protein present on the cell surface of Streptococci. Prevents Complement deposition G-Proteins- Transmembrane signaling surface receptor proteins. Hormones, neurotransmitters etc pass through cell membrane with the help of G proteins Ramachandran Plot- In 1940, Linus Pauling and Robert Corey determined the X ray structure of amino acids to study the conformation of proteins.Based on this, in 1954, Ramachandran and Kartha proposed “Triple helical coiled-coin” structure of Collagen. The protein structure is formed of helix and the formation of helix is due to Steric repulsion between groups of atoms in the polypeptide chains 38. Zinc Finger proteins- Component of Prokaryotic gene regulator. Discovered by Auron Klug in the transcription factor III of Xenopus. It contains Zinc