biochem 3 Flashcards
structure of phospholipids
glycerol
2 fatty acids
a phosphate group
polar end of phospholipid is hydro -
philic
non-polar end of phospholipid is hydro
phobic
phospholipids have 1 end hydrophilic 1 end hydrophobic this is known as
amphiphatic
3 types of steroids
cholesterol
testosterone
oestrogen
sterols are
steroid alcohols
steroid bases with an OH group
steroid structure
base of 4 rings carbon atoms
4 ways lipids can enter body
digested
released from storage
synthesised by liver
phase 1 & 2 fat digestion
in duodenum pancreatic lipase breaks down triglycerides into fatty acids/glycerol
bile salts released to emulsify fat and make more soluble
phase 3 & 4 fat digestion
membrane of small intestine: end products dissolve & diffuse into enterocytes
intestinal lipase helps further digest
fat digestion - at end, what is also formed in entericystes
triglycerides
cholesterol
phospholipids
turned into lipoproteins and go into lacteals of villi
building blocks protein
amino acids
protein formed from which 4 elelemts
carbon hydrogen oxygen nitrogen some also sulphur
which 2 groups does every a/a have
amine group
carboxyl group
each has side chain called
r group - unique
how many a/a found in proteins
20
non-polar a/as are what in water
hydrophobic
polar a/as are what in water
hydrophilic
mnewminoc 20 essental a/as
PVT TIM HALL
PVT TIM HALL
P - phenylalanine V - valine T - threonine T - tryptophan I - isoleucine M - methionine H - histidine A - arginine L - leucine L - lysine
amino acids joined together to make peptides in what reactions
condensation reactions
amino acid bonds called
peptide bond
2 a-as called
di-peptide
aspartame is a peptide made of
aspartic acid
phenylalanine
glutathione dipeptide made of
cysteine
glycine
glutamate
what forms between suphur=containing a/as in tertiary structure
di-sulphide bonds
what happens in denaturation
unfolding of proteins
breaking bonds between SIDE CHAINS making them unable to function
3 denaturing agents
heat
mechanic mixing
strong acids/bases
misfiling caused by
gene mutation
amyloid plaques AD
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
protein, carb and lipid bonds are all formed by what reaction
dehydration synthesis
protein, carb, lipid bonds are all broken down by
hydrolysis
protein digestion 1 - what happens in stomach
HCL converts pepsinogen > pepsin
pepsin breaks protein chains into polypeptides
protein 2 digestion what stimulates pancreatic juices
CCK & Secretin - released in small intestine
3 protein digestion what pancreatic enzymes are released
trypsinogen
chymotrypsinogen
protein digestion 4
what do trypsinogen and chymotrypsinogen get activated into and by wjat
trypsin
chymotrypsin -
by enterokinase in intestinal mucosa
protein digestion 5
action of trypsin & chymotrypsin
chops polypeptides into di & tri peptides in enterocytes
final stage protein digestion
amino acids & small peptides absorbed into blood
