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Purdue BCHM 30700 - Amino Acids
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BCHM 307 1st Edition Lecture 3Outline of Last Lecture I. Oxidation levelsA. Definition of Oxidation II.Hydrophilic and Hydrophobic MoleculesA.Definition of HydrophilicB.Definition of HydrophobicC.Definition of Hydrophobic InteractionsIII. The Hydrophobic EffectIV. Amphiphilic Molecules in WaterV. The Equilibrium Constant and pHVI. Acid Dissociation Contant and pKaA. Definition of Conjugate BaseVII. BuffersOutline of Current Lecture I. Amino Acid BasicsA. Amino Acid StructureII. Amino Acid CharacteristicsA. Definition of ChiralB. Definition of EnantiomersIII. Amino Acid List and AbbreviationsA. Amino Acid GroupsCurrent LectureAmino acids are the basic building blocks of proteins. There are 20 amino acids in biology. All amino acids have the same basic structure. They contain a protonated amino group, an ionized carboxyl group, and a central carbon attached to a hydrogen. The variable R group is what gives the amino acid its unique nature and properties. Almost all amino acids are chiral. Chiral refers to having four different substituents attached to the central carbon atom, making them non-superimposable. The exception is glycine, which has a hydrogen R group. The chirality gives way to two different stereoisomers. Many amino acids are enantiomers. Enantiomers are mirror images of each other; a specific type of stereoisomer. In biology, enzymes have stereospecific binding sites for only 1 of the stereoisomers. Enantiomers can be either L or D. Proteins are made from the L kind. These notes represent a detailed interpretation of the professor’s lecture. GradeBuddy is best used as a supplement to your own notes, not as a substitute.Amino acids and their respective abbreviations are given below in a table.Name AbbreviationsGlycine Gly, GAlanine Ala, AValine Val, VLeucine Leu, LIsoleucine Ile, IMethionine Met, MPhenylalinine Phe, FProline Pro, PSerine Ser, SThreonine Thr, TCysteine Cys, CAsparagine Asn, NGlutamine Gln, QTyrosine Tyr, YTryptophan Trp, WAspartate Asp, DGlutamate Glu, EHistidine His, HLysine Lys, KArginine Arg, RAmino acids can be put into three categories based on their R group properties. The hydrophobic group are those with nonpolar bonds, often C-C and C-H. They avoid water interaction and water will form a shell around these. In this group are alanine, valine, leucine, isoleucine, proline, methionine, phenylalanine, tryptophan, and glycine. Polar uncharged amino acids can’t accept or donate a proton in a solution at physiological pH. Amino acids in this groupinclude: serine, threonine, cysteine, tyrosine, asparagine, and glutamate. The polar, charged group include aspartate, glutamate, lysine, and arginine. Histidine can either be in group 2 or 3. It is dependent on the environment’s pH.Some amino acids have special characteristics. Glycine is the only one without a chiral center. Proline’s R group forms a rigid backbone. It prevents rotational flexibility around the amino group. It will form a kink in a polypeptide chain. Methionine is often used to initiate a polypeptide chain. Leucine and Isoleucine have the same mass. Below are the structures of amino acids covered in this lecture. Only the R groups are written out, the basic structure is designated as


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Purdue BCHM 30700 - Amino Acids

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