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Summary Unit One: Biological Molecules
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water molecules ; CARD HYDRATE 's
Draw a
displayed water molecule
diagram monomers which make up carbohydrates are called monosaccharides
covalent bonds
s
They are formed from Carbon ,
Hydrogen and
Oxygen
s
-
✓
O
S
example =
glucose
> CGHIZOG
-
St
o
H
H H
- St
St -
-
7 alpha
'
glucose
H
bon§
- .
St
You
Hydrogen need to be able to draw this from
memory
As oxygen has free electrons , It pushes the
hydrogen molecules GCHZOH
H 5C O
Closer
together , due to the free electrons
repelling strongly . H
POLAR MOLECULE =
One side of the molecule has a higher positive charge 4C OH H 1C
HYDROGEN BONDS =
The bonds are weak but keep the H2O as a
liquid .
HO 3C 2C OH
H HO
drivers mobsters bet
glucose
m o n o m e rs t
,
2 .
a
MONOMERS =
Small units of On beta CI
which
larger molecules are formed from
glucose ,
the
hydrogen and
hydroxide are reversed on
DIMERS =
TWO monomers
conveniently bonded H HO
/
' SOMER
POLYMERS 7C
Many
=
7C
monomers joined
together
OH H
A condensation reaction Joins monomber with the addition
together
Of a water molecule produced .
Ho - -
OH Ho - -
oh
-
Ee # Aa Ppk Ee DdkAa§BAa ;
n
s -
↳
IDO monomer
a.
t
HO - -
O - -
O - -
O - -
OH
-
dimer
p
-
A
hydrolysis reaction is the opposite ,
it breaks the chemical bond
polymer
between the molecules and
requires H2O instead of
producing H2O
, r.ee#EhEon.*i*EEhEn*o.o*uEa *
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DISACCHARIDES
"
polysaccharides
Joined by a
glycosidic bond Polysaccharides are
polymers made of carbohydrates
formed from a condensation reaction
7. GLYCOGEN
OUEST ION i What disaccharide will be formed ? Stored of alpha glucose in animal cells
GCHZOH GCHZOH Glucose can then be released for respiration
l l
H 5C O H H 5C O H
✓ / Very branched =
Compact , a lot can fit in a small space
4C OHH 7C t 4C OHH 7C
/ /
Insoluble =
Doesn't affect water potential
HO 3C 27 OH HO 3C 27 OH
As
HOH HOH it is
very branched ,
lots of room for enzyme activity
condensation reaction Made of unstructured alpha glucose
(
" " 20 " " "" ° "
Glucose cos 'D "
J
-
a
H 5C O H H 5C O H T BONDS
/ r
4C OH H 7C 4C OH H 7C
\ \ OH
O
HO 3C 2C 3C 2C
(
(
l l
H Ho H Ho 2 .
STARCH
-
mm
HIe@yrezmooIeqf.p
-
there not much difference between starch and
is
glucose
Glycosidic bond ALWAYS forms bet we , Hellcat =
Compact , a lot can
fit in a small space
Insoluble =
Doesn't affect water potential
Maltose >
The
Large big
=
a. alpha glucose t alpha glucose molecule is too to leave the cell
b Sucrose >
alpha glucose fructose
\
. t
C .
Lactose >
glucose tgiactose
Both also 3 . CELLULOSE
-
Debate overt which
type monosaccharides Cellulose is made of beta glucose with
every other one
flipped
Composed of
long straight
,
chains
Linked
Hydrolysis of disaccharides can also occur .
by hydrogen bonds to form fibrils
The Provides
enzymes maltase , lactase and sucrase must be present
strength
HYDROGEN
BONDS
to the
hydrolysis disaccharides above
during digestion
-
occurs ~
iii.it
'
'
[
Mlcrotibril
glycosidic
→ → cellulose
fibril
bonds
, A Ml n 0 a CI d s i sheetmetal ;
The monomers of proteins are cimmino acids A protein is a
polypeptide chain of amino acids
They will
always contain
Hydrogen , carbon ,
oxygen and
Nitrogen
There are around 20
naturally occurring amino acids .
I .
① ⑦ OLD
H O
)
N H C
(
V
H C OH
carboxyl A
primary structure is a
sequence chain of amino acids
v group
A- MIME R GROUP '
found
group on ribosomes
This is the
section that will
change
>
folded in the
rough endoplasmic reti Clum
example =
The R
group for LYSINE is CHzCHzCH2CHzNHz
Whereas the R
group for SY STEINE is CHZSH
H o
2 .
808000000
it
N c
Sulphur Once the structure formed structure can be
H c at
primary
is , a
secondary
g¥ # formed in the shape of A Helix or I
} pleated sheets
i
is :
! ! !!
,
7.7 MONOMER =
One acid I boris
ndrogen
amino
i
x
µ , g
/
2 . DIPEPTIDE =
Two amino acids 1 I '
,
)
! , ↳ Peptide bonds
i
'
3. POLYPEPTIDE =
Multiple amino acids -
Amino acids are Joined via a
peptide bond in a condensation reaction
H o H o 3 .
080080000
N H c N H c After secondary ,
the structure can fold for a third time .
l l
H C C OH -
-
( §µzogy
y - - - - - --
T
! L!
R R Peptide THE ADDITIONAL BONDS
\
, ,
y
µ, gonna, page,
v i i
µ
PEPTIDE BOND i
off of THE R GROUP
-
.
.
, .
.
v
/
hydrogen
-
-
, ypaaohhe.EE#r
Y U Iv ( I / IN
"
:
As stated chains of
previously proteins are
polypeptides long amino
-
There
acids .
They can have multiple structures
by continuing to fold on the are
many different proteins in the
body , all with different shapes
REF >
for
Secondary Tertiary Quaternary
> and Jobs the
.
example ;
Primary
>
.
, top four are
QUATERNARY =
Multiple polypeptide chains bonded a .
Enzymes
to protein b Antibodies
together form a .
c. Transport proteins
bonds present j d . Structural proteins
Once have
the
polypeptides folded to form a
tertiary structure ,
bonds formed based off the R To most be divided into two separate categories
new are amino acids
group .
simplty , proteins can ;
fibrous and globular .
7 . I O n I C
The formation of bonds based off of attractions between
fibrous globulous
negative and positive charges on the R
groups .
Long and narrow Round spherical
Structural purpose functional purpose
2 d l S U l f I Cl e b r i d e s Less sensitive to
changes More sensitive to
changes
g
.
Disulfide bridges are formed when two molecules of the amino in pH and temperature in pH and temperature
acid
cysteine come within close contact -
The sulfur present Insoluble Soluble
in the R
group causes the bonds to be formed .
EXAMPLES =
( on egan EXAMPLES =
Enzymes
and
mycosis and
haemoglobin
3 .
hydrophobic interactions
These bonds are formed between the polar and non -
polar
sections of the molecule .
POLAR distribution of
charge
"
=
molecules with an uneven
NONPOLAR =
WITHOUT dipole dipole interactions
Symetrical molecule -
A
for the stop
malority of proteins , they folding at a
tertiary structure
but a few molecules such as
haemoglobin continue onwards
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