[CHEM 3310] - Midterm Exam Guide - Ultimate 114 pages long Study Guide!

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7 Feb 2017
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CHEM 3310
MIDTERM EXAM
STUDY GUIDE
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\Final Review
Just an overview of some of the high points from each chapter
I. Chapter 1
a. Carbohydrates
i. Glycosidic bond (ether bond) formed by dehydration reaction
ii. Starch: edible, alpha glycosidic bond
iii. Cellulose: inedible, beta glycosidic bonds (beta bad!)
b. Structure equals function!
II. Chapter 2
a. Water
i. High boiling point due to H-bonding
ii. Ionization constant:
1. Kw = 1x10-14 = [H3O+][OH-]
b. Brownian motion: random movement of fluids and gases, powered by
background thermal noise
c. DNA
i. Adenine and Thymine bond together with 2 H-bonds
ii. Guanine and Cytosine bond together with 3 H-bonds
iii. A ad G hae  igs hae   i ae
iv. C ad T hae  ig hae   i ae
v. uracil
d. Hydrophobic Effect
i. Exclusion of nonpolar molecules from the water phase
ii. Inability of nonpolar molecules and hydrophobic molecules to sequester
themselves away from polar water molecules
iii. Entropy driven
iv. No energy required, occurs spontaneously
v. Powers protein folding, creates membranes
e. Henderson-Hasselbalch equation
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i. pH = pKa log [HA]/[A-]
ii. pH=pKa+log[A-]/[HA]
iii. pKA = -log KA and pH = -log [H+]
1. pKA is he thees eatl half oj. ase ad oj. aid
III. Chapter 3
a. Standard AA backbone:
i. Attached to alpha C: carboxylic acid, amino group, alpha H and R group
ii. N, C α, CO
iii. Zwitter ions at physiological pH
iv. pKa of carboxy group in backbone is 3, amine group is 9
1. other pKa values will be given on exam
v. isoelectric point= pI = pH value at which zwitter ion has net zero charge
b. Essential Amino Acids
i. Histidine, isoleucine, leucine, lysine, methionine, phenylalanine,
threonine, tryptophan, valine
ii. The Whole Food Ladder Really Must Have Various Key Ingredients
c. Oxidation-reduction reactions
i. LEO goes GER
ii. OIL RIG
iii. Cells are reducing environments
IV. Chapter 4
a. Protein Structure
i. Pia stutue: seuee of AAs
ii. Secondary structure: localized conformation of polypeptide backbone
1. α helies
a. 3.6 AA/turn
b. prolie is α heli teriator HEAVY GERMAN ACCENT
c. Super secondary: helix-turn-helix
2. beta sheets
a. antiparallel: 2 strands run in different directions
b. parallel: 2 strands run in same direction
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