314 Test 1

Front 1

what is the function of the golgi apparatus

Back 1

this is used for synthesis, modification, and sorting of targeted proteins.

Front 2

what is the function of the lysome

Back 2

this removes waste and is a key in digestion.
-they digest excess/worn out organelles, food particles, viruses, or bacteria.

Front 3

peroxisomes function

Back 3

breakdown of long fatty acids through beta oxidation.

Front 4

function of the nucleus

Back 4

site of synthesis of rRNA and ribosome assembly
---this is where transcription happens.

Front 5

what are the three different kinds of carbohydrates

Back 5

1. glycolipids
-lipids with sugars attached.

2. glycoproteins.
-proteins with oligosaccharides attached.

3. proteoglycans
-proteins with long polysaccharides attached.

Front 6

what is oxidation

Back 6

this is the gain of electrons (it is paired with a reduction reaction, which is the loss of electrons.)

Front 7

what is the difference between an anabolic and catabolic reaction

Back 7

an anabolic reaction requires energy and is endergonic.

---decreases entropy.

a catabolic reaction doesn't require energy and is exergonic.

---increases entropy

Front 8

what is free energy

Back 8

energy that can be used to drive other reactions

Front 9

∆G

-∆G

+∆G

Back 9

∆G-the change in free energy between reactants and products.

-∆G-products have a lower free energy than the reactants.
---this one occurs spontaneously.

+∆G-have higher free energy than the reactants.
---reaction requires energy to proceed.

Front 10

what is a coupled reaction

Back 10

this is when an energetically favorable reaction is used to drive an energetically unfavorable reaction.

Front 11

what are the different kinds of carriers

Back 11

ATP, NADH, NADPH.

---these are temporary stores of energy that drive coupled reactions.

---ATP has high phosphate bonds and NADH/NADPH has high energy electrons.

Front 12

is hydrolysis energetically favorable? why?

Back 12

yes, it is a -change in g.

-it is energetically favorable because it gives a release of unfavorable repulsion by negative charges on terminal phosphates.

Front 13

what is the difference between condensation and hydrolysis

Back 13

condensation requires energy and decreases entropy.

hydrolysis liberates energy and increases entropy.

Front 14

What is an amino group

what is a carboxyl group

Back 14

-NH2

-COOH

Front 15

what is the difference between an acid and a base

Back 15

an acid start with an H and bases has an OH at the end

Front 16

what are the different types of R-groups

Back 16

1. non-polar aliphatic.
-these have equally shared electrons and the carbon atoms form chains.

2. non-polar aromic
-these have a carbon ring that absorbs UV light

3. polar uncharged.
-usually found on the aqueous surface of a protein.
-hydrophilic.

4. polar charged.
-found on the surface of a protein.
-is hydrophilic.

Front 17

what are the 3 types of noncovalent bonds that proteins are held together by.

Back 17

ionic bonds: +-

van der waal interactions: clusters of ch bonds

hydrogen bond: O-H, N-H, F-H.

Front 18

what is a urea?

Back 18

urea denatures proteins; nobody is exactly sure how, but the leading explanation is that it forms hydrogen bonds to the backbone of the peptide backbone.

Front 19

what is a prion

Back 19

this is a virus that causes a rare conformational change in the structure of a protein.
-it even changes the regular protein structures into the prion structure.

Front 20

what is an amylose

Back 20

this is starch; a helical polymer made of glucose units.

Front 21

what is cellulose

Back 21

a linear polymer made of glucose units; bound to each other from beta glycosidic bonds.

Front 22

what are the functions of carbohydrates (sugars)

Back 22

they are used as an energy source to generate ATP.

Front 23

what are polysaccharides used for

Back 23

energy storage and mechanical support (chitin).

Front 24

what is a peptide bond

Back 24

where the carboxyl group of one amino acid is covalently attached to the other amino acid of the other group.

-this is a condensation reaction (gets rid of water).

Front 25

what is the N terminus and the C terminus in a polypeptide

Back 25

this is the polarity of a molecule.

-the N terminus is the amino group (H3N).
-the C terminus is the carboxyl group (COO).

Front 26

What are the four levels of protein

Back 26

1. primary
-a linear sequence of amino acids held together by peptide bonds.

2. secondary
-regular folding arrangements of amino acids.
-there are the alpha helices and beta sheets.
----these arise via H-bonds.

3. tertiary

-3-d shape of the protein that represents its lowest free energy (G).
-this happens spontaneously. (-G)

4. Quaternary.
-the assembly of 2 or more polypeptides.
-they are often held together by covalent bonds.

Front 27

difference between hydrophobic and hydrophillic

Back 27

hydrophobic: insoluble in water (non-polar).
hydrophillic: soluble in water (polar).

Front 28

what is a lipid and what are the three predominant classes of lipids?

Back 28

a lipid is defined by their insolubility in water.

-triacylgycerols (energy storage).

-phospholipids (membranes).

-steroids (cholesterol).

Front 29

what does a triacygycerol look like?

Back 29

Front 30

what does a phospholipid look like?

Back 30

Front 31

what is the most stable state of protein called (lowest energy)

Back 31

the native confirmation.
-these are held together by many weak non-covalent bonds