BIO 320 Lecture2_2009 - SDS-Polyacrylamide gel...

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1 BIO320- 2009 Lecture 2 01/22/09 Protein Structure Alberts, 8-19 SDS-Polyacrylamide gel electrophoresis (SDS-PAGE) Alberts, 8-17 Alberts, 8-18 Alberts, 8-18 SDS-Polyacrylamide gel electrophoresis (SDS-PAGE) Alberts, 8-20 Western Blotting
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2 Composition of a “typical” cell Bonds and Interactions of biological importance ( in order of bond strength) Covalent bond Noncovalent bonds •Ionic bond •Hydrogen bond •van der Walls forces •Hydrophobic interactions Structure of an Amino Acid R-group determines physical properties of amino acid 20 Amino Acids Hydrophobic Hydrophilic Negatively Charged Acid
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3 Positively Charged Basic Unchanged Polar Unchanged Polar - Phosphorylatable! NonPolar Proteins: Chains of Amino Acids Linked by Peptide Bonds Sequence of a peptide •A polypeptide of five amino acids
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4 --is unique for a particular protein. --is critical for the character and activity of that protein. A mutation
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This note was uploaded on 04/12/2009 for the course BIO 50160 taught by Professor O' halloran during the Spring '09 term at University of Texas at Austin.

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BIO 320 Lecture2_2009 - SDS-Polyacrylamide gel...

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