biochem 3 Flashcards

(38 cards)

1
Q

structure of phospholipids

A

glycerol
2 fatty acids
a phosphate group

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2
Q

polar end of phospholipid is hydro -

A

philic

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3
Q

non-polar end of phospholipid is hydro

A

phobic

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4
Q

phospholipids have 1 end hydrophilic 1 end hydrophobic this is known as

A

amphiphatic

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5
Q

3 types of steroids

A

cholesterol
testosterone
oestrogen

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6
Q

sterols are

A

steroid alcohols

steroid bases with an OH group

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7
Q

steroid structure

A

base of 4 rings carbon atoms

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8
Q

4 ways lipids can enter body

A

digested
released from storage
synthesised by liver

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9
Q

phase 1 & 2 fat digestion

A

in duodenum pancreatic lipase breaks down triglycerides into fatty acids/glycerol
bile salts released to emulsify fat and make more soluble

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10
Q

phase 3 & 4 fat digestion

A

membrane of small intestine: end products dissolve & diffuse into enterocytes
intestinal lipase helps further digest

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11
Q

fat digestion - at end, what is also formed in entericystes

A

triglycerides
cholesterol
phospholipids
turned into lipoproteins and go into lacteals of villi

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12
Q

building blocks protein

A

amino acids

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13
Q

protein formed from which 4 elelemts

A
carbon
hydrogen
oxygen
nitrogen
some also sulphur
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14
Q

which 2 groups does every a/a have

A

amine group

carboxyl group

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15
Q

each has side chain called

A

r group - unique

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16
Q

how many a/a found in proteins

17
Q

non-polar a/as are what in water

18
Q

polar a/as are what in water

19
Q

mnewminoc 20 essental a/as

20
Q

PVT TIM HALL

A
P - phenylalanine
V - valine
T - threonine
T - tryptophan
I - isoleucine
M - methionine
H - histidine
A - arginine
L - leucine
L - lysine
21
Q

amino acids joined together to make peptides in what reactions

A

condensation reactions

22
Q

amino acid bonds called

23
Q

2 a-as called

24
Q

aspartame is a peptide made of

A

aspartic acid

phenylalanine

25
glutathione dipeptide made of
cysteine glycine glutamate
26
what forms between suphur=containing a/as in tertiary structure
di-sulphide bonds
27
what happens in denaturation
unfolding of proteins | breaking bonds between SIDE CHAINS making them unable to function
28
3 denaturing agents
heat mechanic mixing strong acids/bases
29
misfiling caused by
gene mutation | amyloid plaques AD
30
7 functions proteins
``` structure body tissues - collagen movement - actin/myosin fibres carier milecules - haemoglobin storage molecules - ferritin fluid balance in blood - albumin enzymes - dig envy,es hormones - insulin immune - complement ```
31
protein, carb and lipid bonds are all formed by what reaction
dehydration synthesis
32
protein, carb, lipid bonds are all broken down by
hydrolysis
33
protein digestion 1 - what happens in stomach
HCL converts pepsinogen > pepsin | pepsin breaks protein chains into polypeptides
34
protein 2 digestion what stimulates pancreatic juices
CCK & Secretin - released in small intestine
35
3 protein digestion what pancreatic enzymes are released
trypsinogen | chymotrypsinogen
36
protein digestion 4 | what do trypsinogen and chymotrypsinogen get activated into and by wjat
trypsin chymotrypsin - by enterokinase in intestinal mucosa
37
protein digestion 5 | action of trypsin & chymotrypsin
chops polypeptides into di & tri peptides in enterocytes
38
final stage protein digestion
amino acids & small peptides absorbed into blood