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DISCOVER

Amino Acids

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Published in: Chemistry
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Amino acids are the building block of proteins.

T H / Kochi

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Qualification: M.Sc, M.Phil

Teaches: Bio Technology

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  1. Aminoacids Aminoacids are a set of 20 different molecules used to build proteins. Proteins consist of one or more chains of amino acids called polypeptides. The sequence of the amino acid chain causes the polypeptide to fold into a shape that is biologically active. The amino acid sequences of proteins are encoded in the genes. Chain Amino Acids Amino Acids Amino Acids Ala: Alanine Arg: Arginine Asn: Asparagine Asp:Aspartic acid Cys:Cysteine General Structure of Amino acids Gin: Glutamine Glu: Glutamic acid Gty: Gtycine His: Histidine Ile: Isoleucine coon Leu: Leucine Lys: Lysine Met: Methionine Phe: Phenylalanine Pro: Proline cys Ser: Serine Thr: Threonine Trp: Tryptophane Tyr. Tyrosisne Val: Valine General Structure Central carbon (co) attached to:
  2. Hydrogen (H) + Amino group (-NH2) + Carboxyl group (-COOH) Side chain (R) 1. Enantiomers: The two non-super imposable mirror images. Molecules are classified as D form (Dextrorotatory ) and L (Laevorotatory) form depending on whether they rotate the plane of plane polarized light clock wise or anticlockwise. 2. Naturally occurring amino acids are L (Laevorotatory) form. 3. D-form aminoacids are rarely found in bacterial cell walls and certain antibiotics (Gramicidin- S, Polymyxin, Actinomycin-D and Valiomycin). 4.N-acetylmuramic acid (NAM) is a D-aminoacid containing tetrapeptide. 5. Peptide bond: covalent bond formed between the u -amino group of one amino acid and u - carboxylic group of other forming a -CO-NH- linkage. H3N—C--COO- + H3i—C--COO- H I Carboxyl Amino terminus terminus Peptide bond Peptide bond + Example of condensation reaction + Exergonic Rigid plannar + Tripeptide means: 3 aminoacids +2 peptide bond 6. All aminoacids have high melting point more than 2000C. 7. Soluble in water and alcohol, insoluble in non-polar solvents. 8. Aminoacids can exist as ampholytes/Zwitter ions.
  3. Amino acids Classification (A) Nonpolar R groups Alanine Va ine (B) Polar R groups Leucine HE—CH tsoleucine Cysteine s Meth onine Proline Phenylalanine Tryptophan Tyrosine Asparagine Glutamine (D) Positively charged R groups Serine Threonine (C) Negatively charged R groups Aspartic acid Glutamic acid Lysine Arg nine His dine Classification of amino acids 20 Different Amino Acids 9. Essential Amino acids: Arginine(Arg/R), Histidine(His/H), Isoleucine (lie/l), Leucine (Leu/L), Lysine (Lys/K), Methionine (Met/M), Phenylalanine (Phe/F), Threonine(Thr/T), Tryptophan (Trp/W), Valine (Val/V). Memory tip: Any Help In Learning These Little Molecule Proves Truly Valuable. This stands for Arginine, Histidine, Isoleucine, Leucine, Threonine, Lysine, Methionine, Phenylalanine, Tryptophan, Valine. 10. Non Essential Amino acids: Alanine(Ala/A), Asparagine(Asn/N), Aspartate(Asp/D), Cysteine(Cys/C), Glutamate(G1u/E), Glutamine(G1n/Q), Glycine(G1y/G), Proline(Pro/P), Serine(Ser/S), Tyrosine(Tyr/Y). 11. Histidine and Arginine are essential amino acids for infants but not healthy adults. 12. Cysteine and Tyrosine are considered to be semi-essential amino acids. They are required by premature infants and adults who are ill.
  4. 13.Simplest amino acid: Glycine- An aminoacid without asymmetrical carbon atom. 14.Acidic aminoacids: Glutamic acid and Aspartic acid Glutamic acid -Most common aminoacid undergo oxidative deamination. 15.Basic aminoacids: Lysine and Arginine Arginine contain guanidium group Histones are rich in basic aminoacids 16. Neutral aminoacids: Glycine, Valine and Phenylalanine. 17. Alcoholic aminoacid: Serine and Threonine. 18. Aromatic aminoacids: Tryptophan, Tryrosine, Phenylalanine Aromatic aminoacids absorb UV —light . This account for the characterization strong absorbance of light by most proteins at wavelength of 280 nm Tryrosine forms skin pigment melanin and two hormones Adrenaline and Thyroxine 19.Heterocyclic aminoacids: Tryptophan and Histidine Tryptophan (Bulkiest amino acid) has indole ring Tryptophan: precursor of IAA (Indole 3-acetic acid- plant hormone) and nicotinamide (a ß vitamin ) Amino acids with buffering activity-Histidine Histidine :only aminoacid having an ionisable side chain with a pka near neutrality (pk value=6.1) Buffering capacity of plasma proteins and haemoglobin is mainly due to Histidine residues Histidine :more present in active site of an enzymes Histidine contain imidazole group Histidine found in intracellular and extracellular fluids of most animals and plants. 20. Sulphur containing aminoacid Cysteine, Methionine 21. Aminoacids with amide group: Asparagine, Glutamine 22. Proline (Secondary imino amino acid) is rarely found within alpha helix segments. 23 Selenocysteine: 21st aminoacid present in human protein.
  5. 24. Un common aminoacids: • Collagen (A fibrous protein of connective tissue): 4 hydroxyproline, 5-hydroxyglycine. • Myosin (A contractile protein of muscle):6-N Methyllysine • Prothrombin (Blood clotting protein):y-carboxyglutamate 25.Non-PROTEIN AMINO ACIDS: Ornithine and Citrulline are involved in the biosynthesis of Arginine and in the Urea cycle. 26. Glutathione is a co enzyme of oxidation —reduction reactions which consist of glutamic acid, glycine and cysteine. This chemical is important in preventing oxidative damage to erythrocytes. 27.Aspartame(Nutrasweet) is artificial sweetner, synthetic dipeptide, chemically it is -L-aspartyl- L-phenylalanine 28. Neurotransmitters: GABA (Gamma Amino Butryic Acid)-a derivative of glutamic acid Dopamine-derivative of tyrosine 29. Histamine- histidine derivative, allergic reaction mediator 30. Amino acids as helix breakers- Proline-Glycine-Tyrosine-Asparagine 31.Bend producing amino acid :Glycine-Proline -serine -Threonine 32.Sickle cell haemoglobin differs from normal haemoglobin by a single amino acid. In the ß chain of sickle cell haemoglobin ,a valine (a hydrophobic acid) has replaced a glutamic acid( a negatively charged amino acid) 33. pl denotes isoelectric point/pH

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