Week 3 Lecture 1, Proteins:

Flow of Information

Protein Functions
-50% of dry mass of a cell is protein.
-Most varied macromolecule in structure and function.
-Acts as the cells infrastructure:
-Enzymes-the machines and factories-catalyze chemical
reactions.
-Structural proteins-the highways and girders.
-Signaling proteins-the cells sensesreceptors and ligands.
Amino Acids
-Proteins are polymers of amino acids
monomers.
-20 different amino acids.
-All amino acids have an asymmetric carbon
attached to
-a hydrogen
-an amino group
-a carboxyl group
-a variable side group (R)

Nonpolar Amino Acids

-Nonpolar=hydrophobic
-Usually in interior of protein.
Polar Amino Acids
-Polar=hydrophilic
-Polar groups from hydrogen bonds

Charged Amino Acids

-Charged=hydrophilic
-Charged groups form ionic bonds
-Charged groups are acid or basic

Linking Amino Acids

-A dehydration reaction links a new monomer
(amino acid) onto the polymer (peptide).
-Linked by a peptide bond.
-The peptide has an amino acid (N-term) and a

carboxyl end
(C-term).
Linking

Amino Acids
-Build proteins from N C.
-Backbone is same for all amino acids added except proline
-Side chain contains the information
1 Structure = Sequence
-For example:
n-ser-phe-leu-pro-thr-his-his-gluy-lys-val-C
-Determined by sequence of bases in DNA and RNA.
2 Structure = Backbone Interactions
- helix is interaction between amino group and carboxyl
group of every 4th amino acid
- pleated sheet is interaction between amino group and carboxyl group of
neighboring chains
-determined by peptide backbone

Structure = R Group Interactions

-Determined by R groups
-Van der Waals Interactions between hydrophobic groups.
-Hydrogen bonds between polar groups.
-Ionic bonds between charged groups.
-Disulfide bridges between cysteine residues.

4 Structure = Multiple Subunits

-Not all proteins have this layer of structure.
-Multiple polypeptide subunits interact to form the
functional protein.
-Determined by backbone and R groups not involved in
lower levels of structure.

The Final Product

Unfolding a Protein
-A protein requires the perfect environment to stay folded and
functional.
-Heat, pH, salt concentration

Week 3 Lecture 2, Nucleic Acids:

Function of Nucleic Acids
-Unique among all molecules because they act as a template for
building.
-DNA DNA and RNA
-RNA protein
Function of DNA
-Deoxyribonucleic Acid (DNA)
-Store and transmit hereditary information.
-Instructions for the functioning of the cell.
-Template for RNA.
-Ribonucleic Acid (RNA)
-Template for making protein (mRNA=messenger RNA)
-Machinery for making protein (ribosome)

Building Nucleic Acids

-Nucleic acids are long polymers of nucleotides.

Nucleotide Backbone
-RNA has ribose sugar
-DNA has a ribose sugar which lacks 2 hydroxyl group
-All nucleotides contain a pentose sugar + phosphate
group (backbone)

Nucleotides vary in the base

cut Py (pie)
pure as (AG) silver

Base Pairing
-Nitrogenous bases hydrogen bond to one another.
-In DNA
-Adenine: Thymine

-Cytosine: Guanine
-In RNA
-Adenine: Uracil
-Cytosine: Guanine
A and T have 2 hydrogen bonds
A and U have 2 hydrogen bonds
C and G have 3 hydrogen bonds

Double Stranded DNA

-All DNA is double stranded.
-2 strands interact in antiparallel fashion.

DNA vs RNA
-Similarities
-Both are built 5 3
-Both are composed of nucleotides (pentose sugar + phosphate
group +
nitrogenous base)
-Both used as a template to make another molecule.