Biochem Exam 3

Front 1

Fatty Acids

Back 1

monocarboxylic acid with hydrocarbon chains that must be at least 12 carbons,
Function Groups: carboxylic acid and acyl chain.

Front 2

Double bonds in hydrocarbon chains.

Back 2

the double bonds are in the cis conf.
Cis form occurs in nature.

Front 3

Triacylglyerols

(Fatty acid)

Back 3

glycerol backbone with 3 fatty acid tails.

for storage and transport in adipose tissue.
insulation
water repellent
not found in membrane.

Front 4

Phosphoacylglyerol

(Fatty acid)

Back 4

glycerol backbone with 2 fatty acids and a phosphate attached.

are present in the bilayer, membrane - are found in the membrane because they are ampiphatic.

Front 5

Wax esters

(Fatty acid)

Back 5

consists of a long fatty acid chain and a long chain alcohol.

forms an ester bond via esterification.

Front 6

Sphingolipids:

Back 6

made up of the sphingosine backbone instead of the glycerol backbone.
The first carbon is a fatty acid chain.
The second is an alcohol.
The third is a amine.
The fourth carbon is also an acohol.

they are ampipathic- so they are present in the bilayer.

Front 7

MP of unsaturated double bonds.

Back 7

unsaturated fatty acids have a lower MP that saturated.

Front 8

Name the two fatty acids that are common in the bilayer.

Back 8

shingolipids
phosphoacylglyerol

Front 9

2 Examples of glycoshingoplipids.

Back 9

cerebrosides - are neutral and contain sugars

gangliosides - have a neg. charge and contain sialic acid.

Front 10

Cholesterol

Back 10

made of terpenes and derived from isoprene units.

4 fused rings with one hydrophobic -OH group. This is hydrophillic due to this group.

Front 11

Terpenes

Back 11

Vit E. is a terpene. Vit. A and Vit K are mixed terpenes.
not found in the membrane.

Front 12

bilayer proteins

Back 12

proteins make of 50 of bilay by weight.

consists of integral and periperal proteins.

Front 13

Peripheral membrane proteins

Back 13

can be removed from the membrane by changing salt conc. and pH.
Loosely associated via noncovalent interactions in H+ bond and electrostatic interactions.

Primarly assocaited with polar groups.

Front 14

Integral membrane proteins

Back 14

proteins with hydrophobic surfaces and nonpolar amino acids associate with the membrane.
have hydrophobic and hydrophillic regions.

detergent is essential for removal.

Front 15

Lipid linked proteins.

Back 15

proteins can be linked to the membrane via acylation, prenylation, or a GPI anchor.

Front 16

Glycosylated proteins on surface of membrane.

Back 16

proteins are glysocylated with sugars to form protective surface by associating with water.

Front 17

liposomes

Back 17

used to deliver hydrophillic molecules like DNA and protein to targeted locations and membranes.

Front 18

3 ways to activate a molecule for a metabolic pathway.

Back 18

1. phosphorylation
2. adding nucleotide
3. acyl-CoA

Front 19

What happens to electrons in a redox reaction.

Back 19

they are donated to a coenzyme and the coenzyme is reduced.

Front 20

Name 3 coenzymes involved in redox reactions

Back 20

NADH
FADH2
CoQ

Front 21

NADH vs. NADPH participate in what specific type of reaction.

Back 21

NADH is catabolic
NADPH is anabolic

Front 22

3 reasons ATP is choosen to store energy

Back 22

cleavage of ATP leads to more products and gives an increase in entropy.

increase resonance with the cleaved phosphate

reduce electrostatic repulsion between adjoining phosphates in ATP.

Front 23

What are the ecosinoids derived from?

Back 23

arachidonic acid - 20 carbons.

Front 24

3 classes of econsanoids:

structure and function
(all hormones)

Back 24

1. prostaglandin
contains a pentane ring.
promoted inflamation, pain, fever, vasoconstriction and vasodilation.

2. thromboxiene
contains a six membered ring containing an oxygen.
6 membered cyclic ether ring.
invovled in blood clotting and inhibited by asprine.

3. Leukotrienes
contain 4 double bonds and 3 are conjugated.
linear structure with no rings.
chemotactic agent and invovled in asthma.

Front 25

enzyme catalyzed reactions are always reversible or irreversible?

Back 25

reversible.

Front 26

Structure of the 4 sugars.

Back 26

glyceraldehyde is a triose.
Glucose is a hexose and an aldehyde.
Galactose is a hexose and an epimer of glucose.
Fructose is a hexose and a ketone.

Front 27

How many carbons do carbohydrates contain.

Back 27

3-9 carbons

formula: (CH2O)n

Front 28

Anomers

Back 28

differ in configuration around the carbonyl carbon.

Front 29

What conf. do sugars usually exist in?

Back 29

D conf.

Front 30

Formation of hemiacetal and hemiketals

Back 30

intramolecular reaction between carbonyl and OH group.

gives the formation of rings.

pyranose- 5 membered rings.
furanose- 6 membered rings.

Front 31

monosaccharides
oligosaccharides
polysaccharides.

Back 31

mono-one sugar unit.
They are linked together via glycosidic bonds.
Oligo- 2-20 sugars
Poly- 20 or more sugars

Front 32

Common disaccharides

Back 32

Lactose- galactose and glucose liked via B bond.
Sucrose - glucose and fructose.
Starch - maltose and is 2 glucoses linked together via and (alph 1,4)
Cellulose - 2 sugars linked via a (beta 1,4)

Front 33

Cellulose

Back 33

in plant cell walls.
homopolysaccharide of glucose linked via a B(1,4) linkage.

Front 34

Chitin

Back 34

structural polysaccharide.
has a similar structure to cellulose that it is a homopolysaccharide of glucose and linked via a B(1,4) linkage.
found in the exoskeleton of insects.

Front 35

Starch

Back 35

storage polysaccharide in plants.
mixture of alpha-amylose and amylopectin.
linked via an alpha(1,4)

digested by alpha and beta amylase.

Front 36

Glycogen

Back 36

storage polysaccharide in animals.

homopolysaccharide composed of glucose.
linked via alpha(1,4) and branch points are alpha(1,6)

Front 37

Peptidoglycan

Back 37

major component in bacterial cell wall.
heteropolysaccharide of repeating NAM and GAG units.

Front 38

Glycoproteins

Back 38

protein with a covalently bonded carbohydrate.

N-linked:
linked in asparagine via an amide bond.

O-Linked:
linked to serine or threonine via a glycosidic bond.
both occur post-tranlationally

Front 39

Function of sugars covalently bonded to protein:

Back 39

affect the 3-D conf. of the protein.
can stiffen and stablize the backbone while shielding it from proteases in the ECM.
Important in protein function and localization in the membrane.

Front 40

Interactions between carbs and protein.

Back 40

Non-covalent include H-bonds, vander waals, electrostatic

Front 41

ABO blood type groups

Back 41

they are included in glycoproteins.
the glycoproteins are antigens on the surface of the cell that is involved in self recognition.

Front 42

Selectins

Back 42

glycoproteins that recognize specific carb. structures.
selectins are located on inside of blood vessel, and participate in the movement of neutrophils along the blood vessel.
the selectins are attaching to vessel and recognize carb. on the surface of the neutrophil allowing it to roll along the surface of the vessel.