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Biological molecules
Proteins
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Cards (14)
globular proteins
compact
spherical
soluble
in water -> orientation of
hydro-interactions
easily
transported
and involved in
metabolic
reactions
folding into specific shapes ->
enzymes
and
active
sites, and
receptors
for
antigens
conjugated protein
contain a
prosthetic
group
haemoglobin
carries
oxygen
as
oxyhaemoglobin
quaternary
structure ->
4
polypeptide chains
2
a-globin
and 2
b-globin
4
globin chains held by
disulfide
bonds
haem
group (
fe2
+) holds
oxygen
function of haemoglobin
transport
oxygen
around the body
soluble
-> more efficient travel in the blood than
oxygen
by itself
each oxygen binds and
alters
the quaternary structure making the next molecule
easier
to bind
insulin
produced by
b-cells
in the
pancreas
control of blood
glucose
two
polypeptide
chains held by
disulfide
bonds
specific structure to membrane
receptors
pepsin
enzyme
suited to
acidic
conditions in the
stomach
fibrous proteins
long
polypeptide
chains with
cross
links
between chains due to
hydrogen
bonding
insoluble
due to the presence of increased
hydrophobic
R groups
highly
repetitive
amino acid sequence ->
organised
structure
(f) collagen
flexible
->
connective
tissues
many
hydrogen
bonds -> increase
tensile
strength
insoluble
-> high length
increases
time taken to
dissolve
present in
artery
walls to withstand
pressure
(f) keratin
strong
large amounts of the
amino
acid
cysteine
which
increases
the amount of
disulfide
bonds
found in
finger nails
and
hair
(f) elastin
connective
tissue
blood vessels ->
stretch
and
recoil
to each
pulse
response
primary structure
sequence
of
amino
acids
with
peptide
bonds between them
secondary structure
beta
pleated sheet
or
alpha helix
hydrogen
bonds
tertiary structure
ionic
and
disulfide
bonds
hydrophobic
and
hydrophillic
interactions
structure of collagen
peptide
bonds between
amino
acids
every third amino acid is
glycine
coils
into a
helix
three
polypeptide chains
hydrogen
bonds between the chains
forms
fibrils