Energy
Enzymes
NA/Carbs
MISC 2
MISC
100

Fill in the blank:

Higher free energy...

-____ stable

-____ concentrated

-____ ordered

-____ work capacity

Lower free energy...

-____ stable

-____ concentrated

-____ ordered

-____ work capacity

**objects tend to move from ___ free energy to ___ free energy!**

Lower free energy...

-___MORE_ stable

-__LESS__ concentrated

-_LESS___ ordered

-__LESSER__ work capacity

Higher free energy...

-__LESS__ stable

-__MORE__ concentrated

-__MORE__ ordered

-__GREATER__ work capacity

**objects tend to move from __HIGHER_ free energy to __LOWER_ free energy!**

100

What is the vmax?

vmax: "point at which all of the enzyme's active sites are full; enzyme is processing substrate to product as fast as it can"

-point of saturation

100
What 3 components make up a nucleotide?

Nucleotide:

-a sugar (ribose = RNA; deoxyribose = DNA)

-a phosphate group

-a nitrogenous base (RNA? DNA?)

100

What is the difference between a phospholipid and a triacylglyceride? Why are they important?

phospholipid has a phosphate-containing compound that replaces 1 fatty acid

-important b/c phospholipids are a major component of biological membranes!

100

What is the chemical difference between reversible and irreversible inhibition?

reversible: non-covalent binding

irreversible: covalent binding

200

Explain the 1st and 2nd laws of thermodynamics

1st Law: energy is neither created nor destroyed, simply changes from one form to another

-ex: kinetic --> potential 

2nd Law: the transformation of energy is associated with an INCREASE in disorder (aka entropy)

200

What is Km? What does a low Km mean? A high Km?

Km: "substrate concentration at which the reaction rate is half maximum (aka 1/2 vmax)"

-low Km: achieves maximum catalytic efficiency at a low substrate concentration (good, very efficient)

-high Km: takes a high substrate concentration to reach maximum catalytic efficiency (bad, not efficient)

200

What are the pyrimidine bases? Purine bases? Which bases pair with what (whose rule is this)?

pyrimidine: thymine, cytosine, uracil (one ring)

purine: adenine, guanine (2 rings)

-Chargaff's rule!

200

Differentiate between saturated vs. unsaturated fats

saturated: lack double bonds; SOLID at RT

-ex: butter

unsaturated: have double bonds; liquid at RT

-ex: oils

200

What is a catalyst? How does it work?

Catalyst:"aka an enzyme, lowers activation energy by stabilizing the transition state"

-catalysts do NOT affect delta G

-catalysts are NOT consumed in the reaction

-catalysts DO speed up the rate of the reaction!

300
Differentiate between an endergonic vs. exergonic reaction.

exergonic: reactants have MORE energy than products; aka spontaneous; energy is RELEASED; delta G < 0

endergonic: reactants have LESS energy than products; aka non spontaneous; energy is ABSORBED; delta G > 0

300

What is a cofactor?

cofactor: small, non-protein molecules; typically inorganic (metal) ions

-ex: Zn+2, Mg+2

-cofactors work to provide a broader range of chemistry at the active site, which allows for enzymes to catalyze a broader range of reactions

300

Describe the sugar phosphate backbone

sugar phosphate backbone:

-has polarity

-5' phosphate end

-3' hydroxyl end

-next nucleotide added to chain is ALWAYS added to 3' OH end

300

Describe cholesterol. What kind of lipid is it?

cholesterol:

-largely hydrophobic, but has a polar head group (what is this called?)

-important component of animal membranes

-increases/decreases membrane fluidity depending on temperature

--> high T: decreases fluidity by reducing mobility of phospholipids

--> low T: increases fluidity by preventing tight packing of phospholipids

300

Explain the induced fit model for enzymes.

Enzyme catalysis = lock and key model, with the enzyme's active site representing the lock & the substrate representing the key

-enzyme structure is DYNAMIC!

-when substrate is bound to active site, the active site changes conformation to form an "induced fit", which allows TIGHTER binding between enzyme & substrate

400

How does protein synthesis occur (many AA --> more ordered, less stable protein)? (hint: what should delta G be)

endergonic reactions are coupled to exergonic reactions, which allows endergonic reactions to take place! need more negative delta G to overcome +G

400

How can Vmax be increased?

bonus: does this also increase Km? why or why not?

Vmax can be increased by increasing enzyme concentration

-this does NOT affect Km b/c it does not alter the enzyme's chemical characteristics, so you would expect the substrate to bind no better/worse than normal

400

What is the basic formula for a carbohydrate? What are the names of bond for each macromolecule?

basic carb formula = (CH2O)n

carbs = glycosidic linkage

lipids = ester linkage

proteins = peptide bond

NA = phosphodiester bond

400

put the following in terms of high to low membrane permeability:

O2, K+, glucose, glycerol

(high) O2, glycerol, glucose, K+ (low)

400
What are the 3 forces that stabilize DNA?

1) phosphodiester bonds

2) hydrogen bonds between bases

3) base stacking contributes to DNA stability

500

Explain the 2 classes of reversible enzyme inhibitors

1) competitive: "bear a close structural/chemical similarity to substrate"

-directly competes with substrate for access to enzyme's active site

-adding extra substrate CAN overcome competitive inhibitor

2) noncompetitive: "NOT similar to substrate"

-bind at location OTHER THAN the active site

-adding substrate CANNOT overcome inhibition (why?)

500

What are the 2 important functions of polysaccharides? provide an example of each. Also, are they alpha or beta polymers?

1) fuel storage (alpha)

ex: glycogen in animals; starch in plants

2) structural integrity (beta)

ex: cellulose in plants (cell walls), chitin (exoskeleton cell walls), peptidoglycan (bacterial cell walls)

500

Explain passive vs. active transport. Put the following into each category and explain:

-simple diffusion

-osmosis

-facilitated diffusion

-primary active transport

-secondary active transport

passive transport:

-simple diff

-osmosis

-facilitated diffusion

active:

-primary

-secondary

500
Draw a [S] vs. V graph in the presence of a competitive inhibitor. What happens to Km and Vmax?

Vmax = same

Km = higher