Bio/Biochem

Question 1

What TYPE of Amino Acids will be hydrophilic?

Answer 1

Those with a charge Basic AA (hist, arg, lys) Acidic AA ( Glutamate, apartate) Asparagine and glutamine

Question 2

What are the four hydrophobic AA?

Answer 2

Alanine, isoleucine, valine, phenylalanine Those with long alkyl chains

Question 3

Which direction does kinesins travel?

Answer 3

toward the positive end of microtubules

Question 4

What direction do dyneins travel?

Answer 4

Towards the negative end

Question 5

Tubulin is polar and has negative and positive sides, where does each connect in mitosis?

Answer 5

Negative at centriole Positive at centrosome

Question 6

What’s the main difference between coenzymes and cofactors?

Answer 6

Coenzymes are organic materials (like vitamins) Cofactors are inorganic materials (like metals)

Question 7

What are the water soluble vitamins?

Answer 7

B and C

Question 8

What is a haloenzyme?

Answer 8

Has all coenzymes/cofactors to get job done

Question 9

What is an apoenzyme?

Answer 9

Does not have coenzymes or cofactors to get job done

Question 10

In michaelis mendal kinetics if the Km is high, what is the affinity of the substrate?

Answer 10

Low

Question 11

Tertiary protein structures are held together mostly by what?

Answer 11

hydrophobic and hydrophilicity

Question 12

What are cadherins?

Answer 12

glycoproteins that hold similar cell types together by calcium mediated adhesion

Question 13

What are integrins?

Answer 13

Binding tag that bind to extracellular matrix

Question 14

What are selectins?

Answer 14

They are very SELECTIVE in that they will only bind to carbohydrate molecules from other cells.

Question 15

What kind of molecules are impermeable to the cell? (3)

Answer 15

Large Polar Charged

Question 16

In G protein-coupled receptors what does Gs do?

Answer 16

Stimulates adenylate cyclase, which increases cAMP

Question 17

In G protein-coupled receptors what does Gi do?

Answer 17

Inhiibits adenylate cyclase, which decreases cAMP

Question 18

In G protein-coupled receptors what does Gq do?

Answer 18

it activates phospholipase C

Question 19

Zymogens are what? how are they named?

Answer 19

Inactive enzymes with -ogen

Question 20

Native page electrophoresis can best compare..?

Answer 20

molecular size or charge

Question 21

SDS page separates by?

Answer 21

Mass

Question 22

Isoelectric focusing separates by?

Answer 22

pI

Question 23

In size-exclusion chromatography what size molecules are slowed down?

Answer 23

Small

Question 24

How does ion-exchange chromatograhphy work?

Answer 24

the beads are coated with a charge and slow the opposite charge down

Question 25

What is edman degradation used for?

Answer 25

To cleave and analyze small proteins, 50 to 70 AA

Question 26

What is the Bradford reagent used for?

Answer 26

It turns blue the more protein you have

Question 27

Nucleosides are missing what?

Answer 27

phosphate group

Question 28

What molecule (during DNA replication) is responsible for relieving the tension from supercoiling?

Answer 28

DNA gyrase or DNA topoisomerase II

Question 29

DNA polymerase reads in what direction? synthesizes in what direction?

Answer 29

3' to 5' 5' to 3'

Question 30

Proteins are __ to \_\_, DNA is __ to \_\_

Answer 30

N to C 5 to 3

Question 31

Pneumonic to remember the stop codons

Answer 31

UAA - you are annoying UGA - you go away UAG - you are gone

Question 32

What does aliphatic mean?

Answer 32

Non-aromatic

Question 33

What is lactose made up of??

Answer 33

Glucose and galactose

Question 34

Which is easier to degrade, alpha helical or beta sheets?

Answer 34

alpha helical. This makes it more soluble

Question 35

Competitive inhibition does what to Km and Vmax?

Answer 35

Km increases Vmax stays the same Affinity changes but saturation stays the same value. Inhibitor binds to the active site because you can outcompete the inhibitor

Question 36

Noncompetitive inhibition does what to Km and Vmax?

Answer 36

Km stays constant Vmax changes The affinity stays the same but because the noncompetitive attacks the allosteric site the max saturation is effected

Question 37

To find the isoelectric point of a neutral AA do what? acidic AA? basic AA?

Answer 37

Add the top and lowest pka divide by two Add the bottom two pka divide by two Add the top two pka's divide by two

Question 38

anode/cathode: Anions (A-) are attracted to ______ and Cations (A+) are attracted to the \_\_\_\_\_\_\_\_

Answer 38

anode cathode

Question 39

What is the difference between an epimer and and an anomer? Both are diastereomers

Answer 39

Epimers differ in chirality at one carbon Anomers differ in chirality at the anomeric carbon ( the carbon that connects a straight chain glucose to a ring glucose)

Question 40

Structure of glucose

Answer 40

CHO | H - OH | HO- H | H - OH | H - OH | CH2OH