Dr. Hoeger’s UCSD Pre-Lecture: O-Chem 2
I like that Professor Carl Hoeger:
a) was able to effectively recap in 2 sentences everything my previous O-chem teachers tried to explain in three months
b) says “damn” during his lecture
Check it out here:
Best NMR Tutorial Ever
GO HERE:
http://www.wfu.edu/~ylwong/nmr/
And look! You can even do a drag & drop exercise!!! *drool*
Infrared: Fingerprint Region
Breakdown of the IR region is as follows:
- Functional Group (4000-1500 cm-1)
- Fingerprint Group (1500-900 cm-1)
- Aromatic (although this is better seen through NMR)
On this entry, we’re concerned about the fingerprint region.
The fingerprint region (1500-900 cm-1) lies between the functional and aromatic regions.
This place is rife with a bunch of complex bands due to the bending vibrations that occur here. NMR now predominates the analysis of this region but the significance of the C-O bond (1300-1000 cm-1) carries some importance here.
“Because the C-O bonds are highly polarized, their absorption bands are generally very strong (254).” But be careful since esters, ethers, and alcohols dwell around this region, too. If you see something in the middle of this region you can bet that a single bonded carbon-oxygen will show up in your molecule.
Mutarotation
Note: This is not required for the MCAT
If you put sucrose in water, its optical properties change. It mutates. Sounds frighteningly boring because it is.
Luckily it doesn’t happen for all sugars. Just the ones where the anomeric carbon is a hemiketal or hemiacetal. Didja get that? You can check out wikipedia for this.
3-Dimensional Structure of Proteins
♪Note: Only 1° and 2° structures are required for proteins on the MCAT
Proteins make up your body. These are what proteins look like.
Primary structure
The order of polypeptides fall under the primary structure.
The primary structure is like the order of letters in a very long word…However, the precise primary structure of a protein is determined not by the random linking of amino acids, but by inherited genetic information (82)
Secondary structure
This involves the twisting of strands and the pleating of β sheets.
Ion Exchange Chromatography
Helps you find the difference between the amino acids by sifting through a resin. If you used a cation exchange resin in which the positively charged cation is exposed:
1. The most negative travels the fastest
2. The least polar travels the slowest
Partially Hydrolizing Peptides
Enzymes cut in certain places only.
Titration of Glycine
Think back to general chemistry. What, you forgot it? Oh well, so did everyone else.
Amino Acids: Acid & Bases
Dude, just accept it. Chemistry is all about acids and bases.