3.Study_Guide_3_Proteins - Study Guide 3 Proteins/structure...

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Study Guide 3 Proteins/structure (Kopachik) Polymer Monomer Condensation reaction Dehydration Hydrolysis Peptide Polypeptide Protein Amino acid Alpha carbon Asymmetric carbon R group Polar R group Nonpolar R group Electrically charged R group Methionine Peptide bond Amino terminal end (N terminus) Carboxyl terminal end (C terminus) Primary structure Secondary structure Beta (β) sheet Alpha (α) helix Tertiary structure Quaternary structure Dimer Tetramer Prosthetic group X-ray crystallography Chaperon proteins chaperonin Denaturation Mutation Sickle cell hemoglobin Beta globin Enzyme Structural protein Storage protein Transport protein Hormonal protein Receptor protein Contractile protein Defensive protein Gene expression protein
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Main points about protein/structure. 1. Proteins are macromolecular non-branched polymers that are made using monomeric amino acids in condensation reactions (specifically a dehydration) creating a peptide bond. They differ in length (number of amino acids), the sequence of amino acids (which of the 20 is used), joining with other polypeptides or prosthetic groups. There are tens of thousands of different types in a typical cell and they are primarily responsible for what a cell does and the greatest diversity of biological macromolecules existing today. 2. There are 20 amino acids differing in the R group which is of one of three classes:
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This note was uploaded on 02/03/2012 for the course BS 111 taught by Professor Patterson during the Spring '05 term at Michigan State University.

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3.Study_Guide_3_Proteins - Study Guide 3 Proteins/structure...

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