Biochemistry 2280A Lecture Notes - Lecture 2: Alpha Helix, Ionic Bonding, Hydrogen Bond

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It is generally stabilized by outside polar hydrophilic hydrogen and ionic bond interactions, and internal hydrophobic interactions b/w non-polar amino acid side chains: e. g. hemoglobin. If the stereoisomers are mirror images of each other, called enantiomers: the only amino acid that doesn"t come in 2 enantiomeric forms is, fischer projection glycine. Is a 2d representation of 3d organic molecules by projection. Isoleucine: most hydrophobic amino acid, branched chain amino acid, aromatic. Its role is coordinating metal ions in proteins like hemoglobin: properties, all contain benzene ring, alternating (conjugated double bonds) delocalized pi electrons, hydroxyl amino acids. Includes: tyrosine, serine, threonine, properties, polar, hydrogen donors + acceptors, form phosphate esters plays important role in signalling, sulfur-containing, cysteine, some similarity with serine, can form weak hydrogen bonds, forms disulfide bonds (stabilises extracellular proteins) Ionisable ( thiolate anion: methionine, fairly hydrophobic, always the first amino acid in protein biosynthesis, basic.

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