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92 Cards in this Set

  • Front
  • Back
Characteristics of water molecules that are believed to be responsible for its
anomalous "behavior."
High boiling point
High freezing point
High heat capacity
Have a dipolar character, which leads to hydrogen bonding
Solid water (ice) is less dense than liquid water, floats
Name the chemical species represented by the formula H3O+.
Hydronium ion
Define the equilibrium constant.
K’eq = [H+][A-]

An expression that indicates the extent of dissociation of the compound AH into A- and H+. It relates the individual ion concentrations to the aqueous compound.
List the ways in which [H+] can influence biological systems.
-Rates of enzyme-catalyzed reactions
-Permeability of membranes to many molecules
-Stability and “native conformation” of proteins and other macromolecules
-Rates of transport of molecules, both charged and uncharged, through membranes
-Absorption, transport and metabolism of drugs
-Hydrophobicity or hydrophilicity of a compound
two most important buffer systems in the body. more important?
Phosphate buffer system: has a pK’ closer to the desired pH of the body, BUT
Bicarbonate buffer system: manages most of the buffering of the blood because of its abundance;
pK's of the bicarbonate and phosphate systems?
Note: the pK’ is the –logK’eq

Phosphate pK’ ≈ 6.7
Bicarbonate pK’ ≈ 6.1

Remember, a compound buffers best at a pH near its pK’
Define "acid" and "base" as usually used in biological systems.
Acid: proton donor
Base: proton acceptor

Mnemonic: BAD (Base Accepts; Acid Donates)
Write the Henderson-Hasselbalch equation, and describe its utility
pH = pK’ + log[base]

Relates the concentrations of the components of conjugate pairs to the pH of their environment.

It allows physicians to calculate acid/base balances in the body.
What are the relative concentrations of conjugate acid/base when pH equals pK?
When the pH equals the pK, the components of the system are present in equal amounts (the concentrations of each conjugate pair are equal).
structure of a molecule, and the pK's of its ionizable groups, molecule's titration curve?.
Look for neutral atom
What defines a lipid?
not water soluble; oily, greasy, waxy. extracted from organisms by organic solvents
classes of lipids
 Fatty acids
 Triacylglycerols
 Phospholipids (and related sphingolipids)
 Steroids
 Eicosanoids
 Vitamins
7. Why are fatty acids named fatty acids? What is “fatty” about them? What is acidic about them?
 Unbranched hydrocarbon chain (hydrophobic), fatty part
 Ionizable carboxyl group (acidic part)
9. Why do triacylglycerols make such a good form of energy storage
Triacylglycerols are also stored in an anhydrous form, whereas carbohydrates are stored with water.
10. What are the roles of glycosphingolipids in humans?
They are responsible for blood groups (including the ABO blood group).
12. Do you expect to find fatty acids or lipid hormones free in the blood? Why?
No; because they are hydrophobic. They must be transported as large complexes with proteins.
13. Describe the lipid bilayer membrane. Name the three classes of lipids of which it is composed.
 Glycerophospholipids
 Sphingolipids
 Steroids
How do you name lipids?
2 ways, omega and p
2 cells types with lots shingolipids?
nerve and RBC
4 roles of steroids? aka cholestorol
digestion, hormones, vitamins, membrane
mech of aspirin action?
inhibits cyclogenase
ATP ideal storage form cuz?
needs enzyme to break bond, stable
what role do cAMP and cGMP have?
Purpose phosphorlation of enzyme
cell growth
3 nucleotide components
Nitrogen bases
C, U, T
Py is single
ribonucleotide or deoxyribonucleotide
ribo has O on 2'
tide is complete,
side no phosphate
DNA, RNA bases
come on tard
H bonds for pairs
AT--> 2
tea for 2
3' to 5' and other is 5' to 3'
DNA at 94 degrees
mod of base affect gene expression? nucleotide not in genes that affects metabolism?
mod on mRNA?
Cytosine methylation,
Methylated G's
Aliphatic Aminos
Glycine, alanine, valine, leucine, proline, isoleucine
Aromatic Aminos
Tyrosine, Phenolalanine, Tryptophan
Basic Aminos
Histadine, lysine, Arginine
Acidic Aminos
glutamic, aspartic, glutamine, aspartine
Maple Syrup Disease?
Valine, Leucine, Isoleucine
Disorders from tyrosine, phenolalanine
tyr: albinism, tyrosis, alcapturia
Cause Pellegra
Tryptophan deficientcy
OH groups?
S groups?
reactions they undergo?
OH: Serine, Thrionine
S: Cytesine, Methionine
S--> disulfide bridges
both like phosphorlation
Essential Amino acids
Pvt. Tim Hall
no G's, no tryrosine, no proline, no serine
4 compounds aminos are precursors
alanine = glucose
glycine = heme, purine
tryosine = thyriod
arginine = NO2
what are proteins made of? unique about their bond?
amino acids, peptide bonds, strong from taotomerization
functions of proteins
enzymes, structural, transport, contractile structures
solubility of proteins
Fibrous and insoluble: i.e. collagen, elastin, and keratin
Globular and soluble: i.e. albumin and hemoglobin
Fibrous and soluble: i.e. fibrinogen
different structures of proteins
primary, secondary, tertiary, quaternary (shapes?)
what are some common mods for proteins?
Acetylation: N-terminal residue of the protein is acetylated, more resistant to degradation
Carboxylation: addition of COOH
Hydroxylation: addition of OH
Glycosylation: addition of glucose
Phosphorylation: addition of phosphate
Disulfide linkages: links parts of the polypeptide chain
Which aminos are commonly phosphoralated
Serine, Threonine, Tyrosine
alpha helix, beta sheet, beta turns?
b sheet--> antiparallel most stable
turns from H bonds
what stabilizes higher order protein structures
H bonding, hydrophobic effects, disulfide bonds, van der walls forces
aminos likely to have charge at neutral pH
Aspartic, glutamic, cytetine, tyrosine (neg)
lysine, argenine, histadine, (pos)
proteins denatured how
heat, pH, detergents, chaotropic agents, organic solvents
Hydrophobic Effect
entropy driven, bring shit together
What is Enyzme>
catalyze reaction, not get used up
enzyme: what does it affect, what not?
activation energy,
not G Keq
Two models how they work and describe, for enyzmes
lock and key--> specificity
induced fit--> catalytic and spec
3 point attachement (ensure steriospecificity)
Prosthetic group, ex?
small nonprotein bound to active sites, complex called holoenzyme
heme, biotin, flavin
6 classes proteins?
transferases, lyases, hydrolases, oxidativereducatases, isomerases, ligases
Michaelis menten equation
V = Vmax [S]
Km + [S]
on michialis menten plot where Vmax and Km
Vmax top
Km half Vmax on X
Lineweaver burk plot also called, what are intercepts?
double reciprocal, X -1/Km
Y 1/Vmax
Eadie Hofstee
spread out data
Competitive inhibitor is different from other inhibitors how?
binds to active site
What different for different inhibitors on lineweaverburk
comp--> Km diff
non-->Vmax diff
un-->both different
what does inhibitor react with for each type?
you know this, unthreesome!
Sigmoid shape in L-B graph shows what (didnt really go over)
positive coopertivity
What are carbohydrates? Aldoses? Ketoses?
Carbohydrates: class of compounds which consist of polyhydroxyaldehydes, polyhydroxyketones and compounds which can be hydrolyzed to give polyhydroxyaldehydes or polyhydroxyketones

Aldoses: monosaccharide with an aldehyde group
Ketoses: monosaccharide with a ketone group
2. What is the most important monosaccharide, and which polysaccharides are made up of this saccharide?
Glucose is the most important monosaccharide. It is a subunit of starch, cellulose and glycogen.
3. Pyran and furan are organic compounds for which what sugar structures are named? How many atoms per ring?
Furan: a 5-membered cyclic structure
Pyran: a 6-membered cyclic structure
4. What is mutarotation, and where does it take place?
Mutarotation involves changes in configuration at the anomeric carbon by ring opening and closing.
5. What are two conformations of 6 membered rings?
chair and boat
sugar acids named?
If the terminal aldehyde is oxidized to an acid, “-aldonic acid”
If the terminal hydroxyl group is oxidized to an acid, “-uronic acid”
If both terminal groupsare oxidized to acids, “-aldaric acid”
7.Name and describe two commonly found modifications of sugars.
Amino sugars: formed when a hydroxyl group is replaced by an amine group
Deoxy sugars: formed when a hydroxyl group is replaced by a hydrogen
8.What is a glycoside and an aglycone?
Glycosides: formed when the anomeric hydroxyl group of a sugar reacts with another hydroxyl compound. The sugar providing the anomeric carbon is the one the compound is named for, the other is known as the aglycone
9.Which of the three most important polysaccharides have alpha linked sugars? Beta linked? What is the importance of this?
Glycogen: has  linkages; forms a tree-like structure (which allows addition/removal of glucose when it’s needed in the body)
Starch: has  linkages
Cellulose: has B linkages; we cannot digest
10.Name three important disaccharides and tell which have alpha or beta linked sugars.
Maltose: 2 glucoses connected by an  linkage
Sucrose: 1 glucose and 1 fructose connected by an  linkage
Lactose: 1 glucose and 1 galactose connected by a B linkage
11.Tell what glycosaminoglycans are, and name two important ones.
Glycosaminoglycans (GAG’s): unbranched polysaccharides made up of repeating disaccharides where one is an amino sugar and the other is a uronic acid
 Hyaluronic acid
 Heparin
12. In the A, B, O blood group substances, where is the difference in the structures of the oligosaccharides located? How many sugars are different?
Difference due to presence or absence of N-acetyl-galactosamine or galactose linked to the penultimate galactose. 1 sugar difference.
Where glycolysis take place?
Gycolysis: starting substrate and possible ending products?
Pyruvate, Lactate
What musst every cell that metabolizes glucose do first? what enzymes do this?
kinases ex first step hexokinase
Commited step of glycolysis:
what is enzyme, substrate, product? ATP?
ATP used
Control factors of gylcolysis
first reaction (hexokinase)
phosphofructokinase (3rd)
last rxn (+) fructose 1-6 biphosphate
(-) ATP
In what steps of gylcolysis is ATP generated?
7th step and last step
3PG and pyruvate
glycolysis steps that cant be reversed for Gluconeogensis?
commited step,
last step,
first step
Types of approaches to get around barriers encountered in reversing glycolytic path?
different locations (ex mitochondria and ER)
different enzymes spec for this
subcellular organelles involved in gluconeogenesis?
ER and mitchondria
malate shuttle is? where take place?
moves malate from inside mitochondria to outside where its converted back to oxaloacetate
how G-6-P convereted to glucose is gluconeogenesis? T1-3 what moves what?
dephosphoralated in the ER by phosphatase in lumenal wall
which enzyme used in gluconeogenesis in mitochondria and cytosol?
malate dehydrogenase
what tissues are capable of carrying out all steps of gluconeogenesis?
liver, kidney, (intestine but no one cares)