Exam #1:  February 17, 2005

1.    Using the Fischer projection, draw and name any five-carbon D-ketose.

2.    Draw the cyclization reaction of any D-aldohexose and name it. How many asymmetric carbons (chiral centers) does this structure have? How many stereoisomers are theoretically possible?



There are 5 asymmetric carbons. Therefore 2^5 stereoisomers (32).

3.    Draw and name a disaccharide.


4.    Identify and describe the biological roles of three (3) polysaccharides.


5.    What is the difference between a proteoglycan and a glycoprotein?
Both are made up of proteins and saccharides. Difference is that in proteoglycans, carbohydrates make up
roughly 95% of the mass. whereas in glycoproteins the bulk of the biomolecule is protein.

6.    What types of linkages connect oligosaccharides to proteins? Draw each using one monomeric unit from each biomolecule.

 
7.     Cellulose and amylose are both homopolymers of glucose, yet they adopt different 3-dimensional structures.
a.    Explain.
a1-->4 linkage permits formation of helical structures, whereas the b1-->4 linkage forms a linear structure
b.    Using two representative sugars, draw the two structures to illustrate the differences (include hydrogen bonding, label the dihedral angles)



8.    Draw a fat containing 12:0, 16:2 (D9,12) and 14:1(D5).



9.    Why do fats make good storage fuels and polysaccharides make good sources of quick energy?
Nonpolar so dont hydrate. Low density, low MW for storage.

10.    Why would storage lipids make bad structural lipids?
nonpolar, whereas structural lipids are amphipathic

11.    How does heparin work to inhibit blood coagulation?
Inhibits blood coagulation by binding to the protein antithrombin, causing antithrombin to bind and inhibit thrombin, a protease essential for clotting
12.    Define amphipathic.
a macromolecule with polar and nonpolar regions

13.  Draw a glycerophospholipid and a sphingophospholipid, where an amino acid is coordinated via phosphodiester linkage. Use a different amino acid for each.

The 'X' group for each should be any amino acid with a hydroxyl side chain (Ser, Thr, Tyr)

14.    Describe how the following affect the solid/liquid transition temperature of a membrane:
a.    Increase on percent of unsaturated fatty acids
decreases packing, order and temp

b.    Decrease in acyl chain length for saturated fatty acids
decreases facial interactions (smaller S.A.), therefore a bit less order and decreases temp

c.    Sterol content is increased
Orders and stabilizes fatty acid chains, increases order and temp

15.    What are membrane rafts and in what ways do they vary compared to the surrounding sea (non-raft) portions of a membrane?
aggregation of long chain sphingolipids, which then select for certain proteins, steroids, etc that further make it a rigid cohesive structure

16.    *Describe a method of studying membrane dynamics and what it would tell you.
FRAP

17.    *Describe how you would purify a membrane protein?
Depends on desription.

18.    What are the two components of an electrochemical gradient?
1. electrical gradient
2. chemical gradient

19.    Describe the following:
a.    Passive transport
Proteins provide a path for charged or polar compounds through the membrane. Usually a downhill process.

b.    Electrochemical gradient
sum of electrical and chemical gradient across membrane

c.    Antiport process
two substrates moving in opposite directions across a membrane. Can be used to balance charge or couple a thermodynamically unfavorable process to on that is favorable.

d.    Secondary active transport
Encompasses antiport process. Occurs when an endergonic (uphill) transport of one solute is coupled to the exergonic (downhill) flow of a different solute that itself was originally pumped uphill by primary active transport.

20.    Calculate the free energy of transport of Ca2+ from inside an organelle and out into the cytoplasm, where:
a.     = -85mV
b.    R=8.315J/K mol, F = 96,480 J/V mol
c.    T@30C
d.    [Ca2+]in = 140mM, [Ca2+]out = 8mM

-7.2 kJ/mol +(-16.4 kJ/mol) = -23kJ/mol