CHEM 1000 Lecture Notes - Lecture 22: Zwitterion, Protein Folding, Carboxylic Acid

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28 Nov 2017
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Chapter 16 Biochemistry
Sections 16.4-16.7 (Proteins and Nucleic Acids)
Chemistry of living things and life processes
Proteins Large biomolecules consisting of long chains of amino acid residues
Enzymes are made of proteins
Amino Acids Contain both an amine and a carboxylate group attached to the same
carbon (20 different amino acids)
Peptide Bond
Dipeptide Formed when 2 amino acids are joined
Tripeptides contain 3 amino acid units
Polypeptides contain 10+ amino acids units
Proteins may contain 10,000+ amino acids units
Zwitterion A compound in which the negative charge and positive charge are on the
different parts of the same molecule
Amino acids tend to exist as a dipolar ion or zwitterion at physiological pH
Peptide Sequences Sequence of the amino acids in a protein is critical
Written from the free amino group (N-terminal) to the free carboxyl group (C-
terminal)
Structure and Function of Proteins
Primary Structure Sequence of amino acids from N-terminal to C-terminal
Aspartic acid-Arginine-Valine-Tyrosine-Isoleucine-Histodine-Proline-
Phenylaline (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe) (D-R-V-Y-I-H-P-F)
Secondary Structure Way the polypeptide chain folds or coils as a result of
hydrogen bonding of the backbone amide groups
Beta-pleated Sheet Intermolecular hydrogen bonding
Alpha Helix Intramolecular hydrogen bonding
Tertiary Structure 3-D shape of a protein
Protein folding creates spatial relationships between amino-acid units that
are relatively far apart in the protein chain
Quaternary Structure 2+ polypeptide chains can assemble into multiunit
structure
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