第二章氨基酸和蛋白质.ppt

Amino acids and structure acids and bases Protein structure myoglobin and hemoglobin collagen Protein purification Chromatography of proteins Electrophoresis of proteins Protein sequencing Basic Structure of an amino acid The two enantiomers of amino acid Enantiomers Enantiomers are molecules that have? opposite spatial configuration are said to be optically active. One enantiomer will rotate polarized light a set number of degrees to the right. This is called the dextrorotatory isomer or (+) isomer. The other enantiomer will rotate the plane polarized light the same number of set degrees in the opposite left direction. This isomer is said to be a levorotatory isomer or (-) isomer. The two enantiomers of an amino acid The 20 standard amino acids Hydrophobic aliphatic amino acids Hydrophobic aliphatic amino acids Hydrophobic aliphatic amino acids Hydrophobic aliphatic amino acids Hydrophobic aliphatic amino acids Hydrophobic aliphatic amino acids Hydrophobic aliphatic amino acids Hydrophobic aliphatic amino acids Hydrophobic aromatic amino acids Hydrophobic aromatic amino acids Hydrophobic aromatic amino acids Polar charged amino acids Polar charged amino acids Polar charged amino acids Polar charged amino acids Polar charged amino acids Polar uncharged amino acids Polar uncharged amino acids Polar uncharged amino acids Polar uncharged amino acids The 20 standard amino acids acids 、bases and pH Buffer Ionization of amino acids acids、bases and pH An acid can be defined as a proton donor A base as a proton acceptor AcidH+ +base E.g: CH3COOH H++CH3COO- NH4+ H++NH3 The pH of a solution is a measure of its concentration of protons: pH=-lg[H+] buffers An acid-base conugate pair can act as a buffer,resisting changes in pH. Ionization Titration curve of glycine Peptide units within a polypeptide Primary structure Disulfide bond Secondary structure Secondary Structure: Polypeptide Chains Can Fold Into Regular Structures Such as the Alpha Helix,