L1-Intro to Protein Structure Methods

L1-Intro to Protein Structure Methods - BIO320- 2009S...

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BIO320- 2009S Lecture 1 Introduction Protein Structure Methods
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Composition of a “typical” cell
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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
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Structure of an Amino Acid
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R-group determines physical properties of amino acid Alberts, Pg. 132-133
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20 Amino Acids structure Hydrophobic Hydrophilic
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Negatively Charged Acid
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Positively Charged Basic
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Unchanged Polar
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Unchanged Polar - Phosphorylatable!
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NonPolar
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Proteins: Chains of Amino Acids Linked by Peptide Bonds
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Sequence of a peptide A polypeptide of five amino acids
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--is unique for a particular protein. --is critical for the character and activity of that protein. A mutation alters the amino acid sequence. The primary sequence of a protein :
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Each Protein has a SHAPE.
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4 Levels of Protein Structure 1 0  Structure = am ino acid sequence joined by peptide bonds. 2
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This note was uploaded on 07/22/2009 for the course BIO 89545 taught by Professor De lozanne during the Summer '09 term at University of Texas at Austin.

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L1-Intro to Protein Structure Methods - BIO320- 2009S...

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