Test 1

Question 0

Equilibrium

Answer 0

No net change in concentration of reactants over products

Question 1

Steady State Equilibrium

Answer 1

Rate synthesis=rate degraded

Question 2

Open system

Answer 2

Exchanges both energy and matter with surroundings

Question 3

Closed system

Answer 3

Exchanges energy but not matter with surroundings

Question 4

Diastereomers

Answer 4

Pairs of stereoisomers that are not enantiomers

Question 5

Enantiomer

Answer 5

Nonsuperimposable mirror images of chiral molecules

Question 6

Configuration

Answer 6

Fixed arrangement of atoms (how they’re connected to one another)

Ex: cis vs trans

Question 7

Conformation

Answer 7

Rotational placement of atoms (where they are in space related to one another)

Ex: boat vs chair

Question 8

Catabolism

Answer 8

Breakdown of biomolecules (spontaneous)

Question 9

Anabolism

Answer 9

Synthesis of biomolecules (uses energy)

Question 10

Strong acid

Answer 10

High Ka, low pKa

Question 11

Weak acid

Answer 11

Low Ka, high pKa

Question 12

Hydrolysis

Answer 12

Breaking a biomolecule by adding the elements of water

Question 13

Condensation

Answer 13

Synthesizing a molecule by removing the elements of water

Question 14

Hydrophobic Effect

Answer 14

Amphipathic molecules clump together in water to maximize hydrophilic-hydrophilic inxns; namely the hydrophobic region gets clumped on the interior

Question 15

Salting Out

Answer 15

Adding salt to a protein solution to cause the protein to precipitate

Question 16

Cationic exchange resin

Answer 16

Negative resin, thus exchanges positive groups (aka cations)

Ex: carboxymethyl cellulose

Question 17

Anionic exhange resin

Answer 17

Positively charged resin that exchanges negatively charged groups (anions)

Ex: diethylaminoethyl Amine (DEAE)

Question 18

Ion-exchange column separates based on:

Answer 18

Net charge of the molecules. The stronger the charge, the longer it stays on the resin

Question 19

Size exclusion chromatography separates based on:

Answer 19

Size. Small things get stuck in the pores and large things come out first

Question 20

Affinity chromatography separates based on:

Answer 20

Affinity for a ligand that is bound to the resin. Stronger the affinity, the slower it elutes; eluted with a ligand gradient

Question 21

CA or Amide? -mate

Answer 21

CA

Question 22

CA or Amide? -ine

Answer 22

Amide

Question 23

pI

Answer 23

No net electric charge

Question 24

Phi

Answer 24

Dihedral angle between N and alpha C

Question 25

Psi

Answer 25

Dihedral angle between alpha carbon and carboxyl carbon

Question 26

Specific Acitivity

Answer 26

Activity of an enzyme per mg of total protein. So mol of reactant transformed/min / mg of enzyme

Question 27

Edman Degradation

Answer 27

Process of removing one amino acid from a polypeptide chain at a time to determine its sequence

Question 28

Ms/MS or tandem MS

Answer 28

One Mass spec breaks down the polypeptide, the other gets Mr recordings

Question 29

Charac of parallel beta sheets

Answer 29

Adjacent sheets go from N to C in the same direction

H bonding is at an angle btwn adjacent sheets

Distance for each repeating unit is 6.5A

Question 30

Charac antiparallel beta sheets

Answer 30

Adjacent sheets go from N to C in opposite directions

H Bonding is linear

Distance for each repeating unit is 7A

Question 31

Beta turn

Answer 31

Common sequence of aa that connects segments of antiparallel beta sheets; usually see G (flexible) and P (stays in cis configuration)

Question 32

Henderson-Hasselbach Equation

Answer 32

pH= pKa + log ([A-]/[HA])

Question 33

Beers Law

Answer 33

A=e(path length)(concentration)

Question 34

pKa of COOH group in an AA

Answer 34

1.8-2.4

Question 35

pKa of NH3 in AA

Answer 35

8.8-11.0

Question 36

Charac of alpha helix

Answer 36

Each repeating unit is 5.4 A apart

3.6 aa per turn

H bonds are parallel to the axis of the helix