IntroductiontoProtein.pptVIP

Introduction to Protein JL LO HC Lee 2000 June-July Gene Protein One gene, one protein ..\talks\protein_3.ps Genotype phenotype ..\talks\protein_4.ps What do proteins do? Everything Structural and Functional Structural blood, muscle, bone, etc. Functional metabolic, neural, reproduction The Genetic Code I 20 amino acids are coded by groups of three bases (triplets or CODONS) Bases are: C, T, U (instead of A), G 4x4x4 = 64 3 are stop codons 61 code amino acids (with degeneracy) The Genetic Code III The Amino Acids Single and 3-letter Codes Aspartic Acid Asp D Glutamic Acid Glu E Phenylanine Phe F Glycine Gly G Alanine Ala A Cysteine Cys C Histidine His H Isoleucine Ile I Lysine Lys K Leucine Leu L Methionine Met M Asparagine Asn N Proline Pro P Glutamine Gln Q Arginine Arg R Serine Ser S Threonine Thr T Valine Val V Tryptophan Trp W Tyrosine Tyr Y Alanine Grey - carbon White - hydrogen Blue – nitrogen Red – oxygen The CORN Law Peptide Synthesis Two AminoAcids = 2 x (CORN) – Dipeptide + Water (NCR) –CO2- + NH3+ –(CRO) = (N – C – R) – C=O | peptide bond H – N – (C – R – O) + H2O Polypeptide – chain of peptides Hydrophobic-Aliphatic Ala(A) Val(V) Leu(L) Ile (I) Mostly are bifurcated except Ala Hydrophobic-aromatic Phe(F) Tyr(Y) Trp(W) Non-polar Neutral-polar side chains Ser(S) Thr(T) Cys(C) Met(M) Asn(N) Gln(Q) Possess hydroxyl group Acidic amino acids Asp(D) Glu(E) Strongly polar nature Catalytic Metal ion binding ability Basic amino acids His(H) Lys(K) Arg(R) Frequently occurring in enzyme Conformationally important Gly(G) Pro(P) G has no side chain P is the most rigid one Peptide Geometry Peptide Torsion Angles Three main chain torsion angle ψ? N - Calpha bond Ψ? C – Calpha bond ω? C – N bond Protein Conformation ..\talks\protein_6.ps ..\talks\protein_7.ps Alpha-he