Topic 3, amino acids and Chromatography

Topic 3, amino acids and Chromatography - Topic 3—Amino...

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Unformatted text preview: Topic 3—Amino acids: the building blocks of proteins Learning Objectives • Be able to define the following terms: amino acid, peptide, protein, side chain/R group, polar, non-polar, hydrophobic, hydrophilic, chromatography • Know which amino acids belong to which class (basic, acidic, polar, nonpolar) • Know the unique roles/attributes of particular amino acids (methionine, cysteine, proline, those with –OH on side group) • Be able to explain how amino acids are bonded together to form a peptide chain and which end gets added onto • Know the 4 parts that surround the central carbon in an amino acid and be able to draw prototypical structure • Understand the utility of different types of column chromatography and be able to design an experiment to purify a protein based upon the particular attributes it possesses (charge, size, hydrophilic/hydrophobic) All proteins are composed of amino acids, just as DNA and RNA are composed of nucleotides Hemoglobin, ribbon model Hemoglobin, molecular model central carbon hydrogen amino R-group carboxy The part that varies!! Always look for 4 elements around central carbon, but orientation can change… Yes. Which? Is this an amino acid? Another way amino acids are commonly shown—showing loss of a proton is more accurate at physiological pH Don’t memorize the structure of each amino acid. Do know which class they belong to and why that is relevant Amino acids with basic side chains (R-groups have a + charge because they have accepted an H) K We commonly use acronyms or single letter codes for amino acids, you do not need to know those versions for this class Amino acids with acidic side chains (R-groups have a carboxylic acid, more commonly shown as a –COO – with the H already donated) Aka Aspartate Aka Glutamate Amino acids with polar but uncharged R-groups. Can hydrogen bond because of –OH, -SH, and –NH 2 groups Amino acids with non-polar (hydrophobic) R-groups. Made of mostly carbons and hydrogens, rings, cannot H-bond. Role of Methionine • Methionine is the first amino acid in every peptide chain because it is encoded by the start codon (AUG) – However, sometimes peptides have amino acids removed after synthesis in order to become activated/functional • Since methionine contains sulfur, S 35 commonly used to label proteins Cysteine is the only amino acid that can form disulfide bonds,...
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Topic 3, amino acids and Chromatography - Topic 3—Amino...

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