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Lecture

Lecture 3


Department
Biology
Course Code
BIO130H1
Professor
Jane Mitchell

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Lecture 3 (P2) Jan. 19/12
Introduction to Nucleic Acids and Proteins (P2)
DNA structure
Double helix strands are antiparallel, complementary
One strand runs in 5’-3’, other in 3’-5’ (represent carbon # in sugar)
5’ carbon attached to PO4, 3’ attached to OH
Backbone has a polar charge (hydrophilic)
DNA Denaturation
Heat breaks H-bonds between bases
Used in PCR, massive copying of a specific portion in a DNA sequence
PCR uses a primer, which is a strand of nucleic acid that binds to a specific section of
DNA
Primer acts as complementary strand
Denaturation is reversible
Protein Structure
Primary – AA sequence
Secondary – alpha helix, beta sheet
On slides Etc.
Amino Acid intermolecular properties
Basic/acidic (charged)
Uncharged polar, non-polar
Influenced by R group
Polar groups found on protein exterior (aqueous environment interaction)
Non-polar groups found on protein interior (forced away from aq environment)
Intermolecular Synthesis of Proteins
For primary structures
Amino acids undergo a condensation reaction (water comes out)
Creates a covalent peptide bond
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