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Psych Final > Bio Test 1a > Flashcards

Bio Test 1a Flashcards

1
Q

aldehyde group

A

where a c double binds to oxygen and single bonds to hydrogen

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2
Q

ketone group

A

where a carbon is double bonded to oxygen

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3
Q

amphipathic

A

when one side of fatty acid is hydrophillic and the other is hydrophobic

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4
Q

triglycerides

A

have a glycerol backbone

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5
Q

saturated fat is

A

a semi-solid at room temp

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6
Q

unsaturated fat is

A

a fluid at room temp

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7
Q

isoprene

A

cholesterol and testosterone

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8
Q

biological functions of lipids

A
  1. phospholipids are main structural function of membranes
  2. fats are source of energy
  3. fat-soluble vitamins (A,D,E,K) are essential nutrients stored in liver and fatty acids
  4. cell signaling
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9
Q

lipase

A

enzyme that breaks down fats

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10
Q

cell membrane

A

5 nanometers thinks, hydrophillic head and hydrophobic fatty acid

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11
Q

phosphate that is on the extracellular side of cell

A

phosphatidylcholine

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12
Q

phosphate that is on the cytosolic side of cell

A

phosphatidylinositol

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13
Q

what is the cell membrane made up of?

A

phospholipid
cholesterol
glycolipid

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14
Q

What is in the major component in the cell cortex?

A

Spectrin

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15
Q

what do membrane domains do?

A

are locally confined and form functionally specialized regions

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16
Q

what are the membrane domains?

A

cell cortex
extracellular matrix
sharing proteins with other cells
diffusion barrier

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17
Q

intestinal epithelial cell

A

divided into apical and basolateral domains

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18
Q

detergents are…

A

ampipathic (ex: SDS and Triton X-100)

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19
Q

basic structure of lipids

A

glycerol and fatty acid

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20
Q

head of lipid is made up of:

A

polar group, phosphate and glycerol

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21
Q

cells are asymmetrical because…

A

phosphatidycholine is more abundant on the extracellular side and phosphatidylinositol is more abundant on the cytosolic side

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22
Q

protein structure

A

alpha carbon in middle, an amino group, a carboxyl group, a side chain

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23
Q

how many acidic proteins? what are they?

A

2: Aspartic acid and glutamic acid

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24
Q

how many basic proteins? what are they?

A

3: arginine, lysine and histidine

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25
Q

how many polar proteins? what are they?

A

5: asparagine, glutamine, serine, threonine and tyrosine

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26
Q

how many nonpolar proteins? what are they?

A

10: alanine, glycine, valine, leucine, isoleucine, proline, phenylalanine, methionine, tryptophan and cysteine

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27
Q

aspartic acid

A

acidic, asp, D

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28
Q

glutamic acid

A

acidic, glu, E

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29
Q

arginine

A

basic, arg, R

30
Q

lysine

A

basic, lys, K

31
Q

histidine

A

basic, his, H

32
Q

asparagine

A

polar, asn, N

33
Q

glutamine

A

polar, gln, Q

34
Q

serine

A

polar, ser, S

35
Q

threonine

A

polar, thr, T

36
Q

tyrosine

A

polar, tyr, Y

37
Q

alanine

A

nonpolar, ala, A

38
Q

glycine

A

nonpolar, gly, G

39
Q

valine

A

nonpolar, val, V

40
Q

leucine

A

nonpolar, leu, L

41
Q

isoleucine

A

nonpolar, ile, I

42
Q

proline

A

nonpolar, pro, P

43
Q

phenylalanine

A

nonpolar, phe, F

44
Q

methionine

A

nonpolar, met, M

45
Q

tryptophan

A

nonpolar, trp, W

46
Q

cysteine

A

nonpolar, cys, C

47
Q

what are the two ends of an amino chain?

A

amino terminus and carboxyl terminus

48
Q

the amino acids are attached by what kind of bonds?

A

peptide bonds

49
Q

Why do the amino chains go through condensation when connecting to eachother?

A

This is because they have to lose a water molecule in order to attach.

50
Q

What are the five forces that form the structure of amino acids?

A 
hydrogen bonds
disulfide bridge or covalent bonds
ionic bonds
van der walls attraction
hydrophobic force
51
Q

what is the primary structure of proteins?

A

amino acid sequence

52
Q

what is the secondary structure of proteins?

A

alpha helix and beta sheet

53
Q

dimer

A

protein made of two identical proteins

54
Q

tetramer

A

protein made of four identical proteins

55
Q

alpha helix

A

formed by many hydrogen bonds, lots of space and flexibility

56
Q

beta sheet

A

formed by many hydrogen bonds, hold sheets together, very strong

57
Q

denaturation

A

when a material comes in contact with protein and unfolds it

58
Q

chaperones

A

assist protein folding in the cell

59
Q

prion proteins

A

special infectious mis-folded proteins, cause scrapie and mad cow

60
Q

functions of extracellular proteins

A 
structural proteins (collagens)
enzymes (lysozyme)
growth factor (fibroblast growth factor)
immune response (antibodies)
61
Q

functions of membrane proteins

A 
transporters (ion channels)
anchors (integrins)
receptors (growth factor receptors)
enzymes (adenylyl cyclase)
recognition (glycoproteins)
62
Q

functions of intracellular proteins

A 
enzymes (catalase)
structural proteins (actin filament, spectrin)
motor proteins (myosin)
receptors (hormone receptors)
signal transduction (kinase)
special functions (DNA binding proteins)
63
Q

antibody

A

called immunoglobin (Ig), has unique Y shape, tetramer composed of two short chains and two long chains, variable domain on ends of Y where specific antigens bind

64
Q

centrifugation

A

process by which you take a sample of something and separate its contents by size and density

65
Q

homogenization

A

plasma membrane of cells can be ruptured so cell contents can be released to create extract

66
Q

types of homogenization

A

ultrasound
detergent
force cells through small hole
grinding by plunger in tight-fit tube

67
Q

types of chromatography

A

ion exchange chromatography
gel filtration chromatography
affinity chromatography

68
Q

ion exchange chromatography

A

separates proteins by charges

69
Q

gel filtration chromatography

A

separates proteins by size

70
Q

affinity chromatography

A

separates proteins by the binding capacity to the packed protein

Psych Final (21 decks)

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