Bio Test 1a Flashcards

(70 cards)

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
how many polar proteins? what are they?
5: asparagine, glutamine, serine, threonine and tyrosine
26
how many nonpolar proteins? what are they?
10: alanine, glycine, valine, leucine, isoleucine, proline, phenylalanine, methionine, tryptophan and cysteine
27
aspartic acid
acidic, asp, D
28
glutamic acid
acidic, glu, E
29
arginine
basic, arg, R
30
lysine
basic, lys, K
31
histidine
basic, his, H
32
asparagine
polar, asn, N
33
glutamine
polar, gln, Q
34
serine
polar, ser, S
35
threonine
polar, thr, T
36
tyrosine
polar, tyr, Y
37
alanine
nonpolar, ala, A
38
glycine
nonpolar, gly, G
39
valine
nonpolar, val, V
40
leucine
nonpolar, leu, L
41
isoleucine
nonpolar, ile, I
42
proline
nonpolar, pro, P
43
phenylalanine
nonpolar, phe, F
44
methionine
nonpolar, met, M
45
tryptophan
nonpolar, trp, W
46
cysteine
nonpolar, cys, C
47
what are the two ends of an amino chain?
amino terminus and carboxyl terminus
48
the amino acids are attached by what kind of bonds?
peptide bonds
49
Why do the amino chains go through condensation when connecting to eachother?
This is because they have to lose a water molecule in order to attach.
50
What are the five forces that form the structure of amino acids?
``` hydrogen bonds disulfide bridge or covalent bonds ionic bonds van der walls attraction hydrophobic force ```
51
what is the primary structure of proteins?
amino acid sequence
52
what is the secondary structure of proteins?
alpha helix and beta sheet
53
dimer
protein made of two identical proteins
54
tetramer
protein made of four identical proteins
55
alpha helix
formed by many hydrogen bonds, lots of space and flexibility
56
beta sheet
formed by many hydrogen bonds, hold sheets together, very strong
57
denaturation
when a material comes in contact with protein and unfolds it
58
chaperones
assist protein folding in the cell
59
prion proteins
special infectious mis-folded proteins, cause scrapie and mad cow
60
functions of extracellular proteins
``` structural proteins (collagens) enzymes (lysozyme) growth factor (fibroblast growth factor) immune response (antibodies) ```
61
functions of membrane proteins
``` transporters (ion channels) anchors (integrins) receptors (growth factor receptors) enzymes (adenylyl cyclase) recognition (glycoproteins) ```
62
functions of intracellular proteins
``` enzymes (catalase) structural proteins (actin filament, spectrin) motor proteins (myosin) receptors (hormone receptors) signal transduction (kinase) special functions (DNA binding proteins) ```
63
antibody
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
centrifugation
process by which you take a sample of something and separate its contents by size and density
65
homogenization
plasma membrane of cells can be ruptured so cell contents can be released to create extract
66
types of homogenization
ultrasound detergent force cells through small hole grinding by plunger in tight-fit tube
67
types of chromatography
ion exchange chromatography gel filtration chromatography affinity chromatography
68
ion exchange chromatography
separates proteins by charges
69
gel filtration chromatography
separates proteins by size
70
affinity chromatography
separates proteins by the binding capacity to the packed protein