, IA : CHEMISTRY FOR BIOLOGISTS
-
A basic unit
of all matter is the atom
Majority of
atoms do not contain a
full outer shell
of electrons , making them unstable
Through bonding ,
atoms are able to acheive a
full outer shell and become stable
Ionic and Covalent Bonding
Ionic where electrons from
bunding metal to non-metal
is are
transferred a a
covalent bonding is electrons shared
where are
equally among two non-metals
-Electrons become distributed
may fail to
equally , creating a
dipole nature in Substance;
> This the substance
results in
polarity of a
Water
blater is a
dipolar molecule
(This is due the electrons being held closer to the atom than to the
to
oxygen
hydrogen atoms .
(oxygen has a
stronger attraction
compared to the hydrogen)
An bonds
> effect of this
polarity is that water molecules form hydrogen
1 The Molecule will
negative oxygen atom
of One water attract the
positive
hydrogen atoms of other water molecules in a weak electrostatic attraction called a
hydrogen bond
Importance of kater
Transport medium/polar
·
Solevent
-Enables dissolve
many substances in it due to its
polarity
>Ionic substances such as Sodium Chloride will dissolve in it .
covalently bunded substances
are also and dissolve in water well
polar will as
·
water's Maximum density is at 4
> This makes water
widely spread this makes ice denser than water therefore
the water underneath to become frozen This
preventing . allows
organisms to live in
polar regions
·
Cohesive (attraction water molecules together)
of
The stick the
molecules
together , allowing for movement of water
from roofs to rest of
the
plant
Adhesive
>water be attracted different
molecules can to molecules which is
important for transportation
·
Liquids cannot be
compressed
>Benefiting to the
hydraulic System
, High Specific
·
heat
capacity
Temperature of water bodies don't change drastically throughout the
year Creating
, a stable env.
has
· klater a
high surface tension
<This is
important in
plant transport systems as the tension creates a
"pull" on the water
to travel the leaves
that enables it upwards from the roots to
Biological Molecules
Biological are molecules and in living that contribute to
·
molecules ions
organisms various
biological processes such as metabolism and cell division
·
Most
biological molecules are
organic compounds (mostly made of carbon atoms)
up
·
Each Carbon atom ean make
four bonds
>
Therefore it can connect to four other atoms , making long chains
·
Monomers are the smaller units from which larger molecules are made
·
Polymers are molecules made from a
large number of monomers joined together in a chain
The three
major classes
biological molecules are : The
process of
·
of
monomers bonding
>
Carbohydrates with
units to
many reiseating
s
>
Lipids polymers called
>Proteins polymerisation
Carbohydrates
·
Carbohydrates are
biological molecules
important as an
energy source in cells
It
· is made up
of Carbon , hydrogen and
oxygen
atoms
>
They can be
represented by the
formula (xCH2dy
·
There are three main
types of Carbohydrates :
> Monosaccharide
>Disaccharide
>
Polysaccharide
Monosaccharides
They are
·
simple sugars
> There is one
oxygen and two
hydrogen atoms for each Carbon atom in the molecule
The [CHedn
general formula
·
is
·
Triose
Sugars (n
=
3) have 3 Carbon atoms (C3HsO3)
> breaks down triose
They are
important in mitochondria where
respiration glucose into
sugars
·
Pentose Sugars (n=ct have 5 carbon atoms (C3H100s)
>Examples are ribose and deoxyribose which are important in nucletic acids DNA and RNA
, ·
Hexose (n=6) have [C6H1202)
Sugars six carbon atoms S
> Includes
glucose , galactose and fructose
-Glucose has two isomers
they differ in only the location of
> the Hand to carbon 1
I
-glucose OH attached
groups
>A glucose has the H above carbon and the OH below
group
B-glucose
1
,
B glucose has this reversed
Disaccharides
·
Disaccharides consist two monosaccharides joined together , their is
quick-source of energy
of purpose
Two monosaccharides condensation to disaccharide
join in reaction
form molecule
-
a and
a , a
of
water is released
The bond called bond
formed between the monosaccharides is a
glycosidic
>Numbers are used to show which carbon atoms are involved in the bond
·
Three common disaccharides are
> maltose
glucose +
glucose
lactose
>
glucose +
galactose
>Sucrose
glucose fructose
+
Polysaccharides
·
Formed
by the bond of many monosaccharides joined by glycosidic bonds in a condensation run
Its and
primary functions to structure
·
are for energy storage give
They create
very compact molecules which take little
·
,
up space
·
Polysaccharides are
physically and
chemically inactive
do
s o
they not interfere with the other functions of the cell
Examples polysaccharides are
·
:
of
> cellulose
-Starch
>glycogen
is
·
Starch
important as an
energy store in
plants
It be broken
- can
rapidly down to release
glucose when needed
unbranched between
Amylose is an
polymer of 200 - 500 units
of glucose
·
have bond
They a 1-y
glycosidic
-Amylopeptin branched that be broken down to release needed
is a
polymer can
energy when
>Both 1,4 and 1
,
6
glycosidic bonds are
present
Glycogen is
important in
animals/fung
·
:
an
energy storage
>they have them
many glucose units
making very compact
have bonds
> more 1,6
glycosidic
, Lipids
Lipids which contain
hydrogen and atoms (lower (2)
macromolecules carbon
oxygen proportion of
·
are
,
Not a
polymer
·
They are non
polar and
hydrophobic
·
When oxidised their bonds broken S' Had
lipids during respiration are to release CO2
·
are
,
The
·
two
important groups of lipids are :
> Fats
> Oils
Fats animals
are
mostly from
-
solid
They are at room
temperature
-
oils are
mostly from plants
They are
liquids at room
temperature
Fats and oils made triglycerides
mainly of
·
are
up
·
A
triglyceride consists
of a molecule
of glycerol with three
fatty acios attached
25H803
Glycerol
carbony
Hydro-200H group
Fatty acid >
ester
bond
condensation/
-e-
n - - on or
*
R
esterification
H
di o -C
s
R
!
I
- -
-
0H Or -e R I
iP
H - -
H -p
&H OH e R
hydrolysis - 0 -
e - R
H 2
- - -
-
I H -
e -
- -
R
I
3 H
glycerol fatty
acids t
riglyceride
fatty acids and
glycerol combined bonds
·
are with ester
The bond
formed in condensation reaction between the
carboxyl fatty acid
-
is a
group of a
and one of the
hydroxyl groups from each acid
-A molecule of water is removed the bond created is called an ester bund
-This condensation reaction is called esterification
Triglucerides lipids that store
·
are
energy
Phospholipids are
lipids that form membranes
·
Test emulsion add to ethand and
lipids test mix add water
-
for are : -
,
to
-milky white
droplets formation indicates
positive
, Proteins
Proteins are macromolecules and are
important in nutrition
-Proteins have a
variety of roles
including :
needed
>Making enzymes for metabolism
>Make hormones
up
>Make antibodies
Amino blocks
acids the
building proteins
·
are
of
condensation
They together in
-
join reactions
The
general formula Amino acid :
for
-
does not
in
*
R &
>Amino acids contain amine
groups
(-NH2),
participate ran
2"
I
H-N-e
-
OH
Carboxylic acid (-COOH)
groups and
-
a
between
may vary
H carboxyl Side chain which is shown as
[
amino acids
Amino
group
group
Bonding in Proteins
Peptide bonds
The bonds in between acids called bonds
amino
peptide
·
proteins are
·
A
dipeptide bond is
formed when 2 amino acids are involved
bond acids involved
A
polypeptide is when
many amino
·
are
-OH
R O
↑ 11
H
N-
H -
-
-
+ - -
I
R
R P
I e-
H-N - e- C
- - -
N -
e -0H +
H20
I A
i H it it
Peptide
bond
-
Peptide bonds are
strong
Disulfide Bond
Occurs acids that the
only in Certain amino
cysteine
·
is
> The amino acid should contain a
sulfhydryl /-SH)
group
The 3H linked dithol by oxidation
groups are
covalently as a
Disulphide bonds be
formed between different chains ofamino acids between different
-
or
may
the chain
parts of .
, It provides some
rigidity to the molecule
-
protein
Hydrogen bund
·
This is formed between a
hydrogen bond and an
electronegative atom like
oxygen nitrogen ...
-It the between
is
electromagnetic attractive interaction
polar molecules ,
in which
hydrogen is
bound to a
highly electronegative atom
Amino acids with Side chains
containing -NHz in
H-bonding
·
OH etc
participate
-
..
,
-
It is a weak bond
O
21
N-2 -
C -
in
e -
H -
0
H
C
H
H 0
"Ange
H
St
trugen
bond
-
-
-
-
Ionic bund
formed between acids
oppositely charged amino
·
>Van der Wals force is a transient ,
weak electrical attraction
of one atom to another
-
CH2-CH2-CH2 -NHS -
↑
-
O-8-etz-
Tonic
bond
Hydrophobic bond
Created between two
polar groups hydrophobic amino acids
·
non or
-forms interior hydrophobic protein side chains
an , core ,
where most
hydrophobic can
closely associates
Sheilded
are
from interactions with Solvent water
CH
/
HyC CH3
H32 CH3
-
I
CH
, Protein Structures
Primary Structure (i)
·
Based the the amino acids found the
on
sequence of in
proteins
and
3 The
Sequence determines the
shape function of the
protein
(i)
Secondary structure
The localised
shape protein
·
of a
secondary structures can either be:
X-helix-formed due between
> to
hydrogen bonds
forming the
Oxygen of the -co
group
of one amino acid and the
hydrogen of the -NH
group of the amino acid
four
p
laces ahead of it (every fourth pepticle bond)
This
folding
-
causes a
>B-pleated sheet -
a looser
shape from an & helix
this occurs when the
hydrogen bonds are not
strong enough to
form an a-helix
Tertiary Structure (3)
The three-dimensional
which
protein coils to form shape
·
in
way a a
percise
-Four bonds are
responsible for maintaining their
tertiary structures :
>Hydrogen bonds Ionic bonds
>
Disulfide bonds bonds
>
>Hydrophobic
Quaternary Structure (ii)
When
·
two chains associated
or more
polypeptide join together or are with each other
The chains held bonds
together by the for tertiary
are also same structures
Types of Proteins
Fibrous
proteins
like
-Strand
shape
Typically multiple ,
Strands join to
form a
fibrous protein
covalent bunds and
disulfide bridges are
found in them
-
Hydrogen bonds are also
present
-
Examples of fibrous proteins
:
-
>Collagen
> Keratin
> elastin
-
Insoluble in water
, bones
-
found in connective tissue ,
tendons and
to
contains little no
tertiary structures
Globular
protein
·
Has a
Spherical shape
·
Hydrophillic amino acids are
found on the exterior of the
shphere
-Enables the to
protein interact water
with
Hydrophobic amino acids
found the interior
·
are in
soluble water
-
in
-Examples of globular proteins
> Plasma
proteins
>
Enzymes
>
Haemoglobin
to
Contains tertiary quaternary structures ,
allowing them fold into
globular shapes
-
and
cannot be
easily separated
·
Have due the
Carbonyl and Amino ends
ionic
properties to
conjugated proteins
A that combined with another molecule
protein
·
is
The other molecule attached to the called the
protein
is
prosthetic
·
group
- It can be :
>Organic
-
Carbohydrate -
Nucleic acid
Lipid
-
>
Inorganic Iron
-
Carbohydrate
+
protein Glycoprotein
Lipid
+
protein
>
Lipoprotein
Nucleic acid +
protein >Nucleoprotein
Iron+ Haemoglobin
protein
-
The (LDLs)
two
forms of lipoproteins : Low
density lipoproteins
(HDLs)
High density lipoproteins
Collagen
-
Provides
strength to
your
tendons , ligaments , bones and Skin
-Has tensile similar to steel
a
Strength
Very important structural
protein in vertebrates
formed from three
polypeptide chains held
by hydrogen bonds to
form a
triple
helix
Ctropocollagen)
, Haemoglobin
- Has a
quaternary structure
-Made two a subunits two subunits
up of and
2
B
↳
&
⑳
->
2
Fe prosthetic
+
group
connected by bond
a
disulphide
-Both a
globular protein and
conjugated protein
Chaem)
Each
polypeptide chain
surrounds an iron
containing group
-
-
A basic unit
of all matter is the atom
Majority of
atoms do not contain a
full outer shell
of electrons , making them unstable
Through bonding ,
atoms are able to acheive a
full outer shell and become stable
Ionic and Covalent Bonding
Ionic where electrons from
bunding metal to non-metal
is are
transferred a a
covalent bonding is electrons shared
where are
equally among two non-metals
-Electrons become distributed
may fail to
equally , creating a
dipole nature in Substance;
> This the substance
results in
polarity of a
Water
blater is a
dipolar molecule
(This is due the electrons being held closer to the atom than to the
to
oxygen
hydrogen atoms .
(oxygen has a
stronger attraction
compared to the hydrogen)
An bonds
> effect of this
polarity is that water molecules form hydrogen
1 The Molecule will
negative oxygen atom
of One water attract the
positive
hydrogen atoms of other water molecules in a weak electrostatic attraction called a
hydrogen bond
Importance of kater
Transport medium/polar
·
Solevent
-Enables dissolve
many substances in it due to its
polarity
>Ionic substances such as Sodium Chloride will dissolve in it .
covalently bunded substances
are also and dissolve in water well
polar will as
·
water's Maximum density is at 4
> This makes water
widely spread this makes ice denser than water therefore
the water underneath to become frozen This
preventing . allows
organisms to live in
polar regions
·
Cohesive (attraction water molecules together)
of
The stick the
molecules
together , allowing for movement of water
from roofs to rest of
the
plant
Adhesive
>water be attracted different
molecules can to molecules which is
important for transportation
·
Liquids cannot be
compressed
>Benefiting to the
hydraulic System
, High Specific
·
heat
capacity
Temperature of water bodies don't change drastically throughout the
year Creating
, a stable env.
has
· klater a
high surface tension
<This is
important in
plant transport systems as the tension creates a
"pull" on the water
to travel the leaves
that enables it upwards from the roots to
Biological Molecules
Biological are molecules and in living that contribute to
·
molecules ions
organisms various
biological processes such as metabolism and cell division
·
Most
biological molecules are
organic compounds (mostly made of carbon atoms)
up
·
Each Carbon atom ean make
four bonds
>
Therefore it can connect to four other atoms , making long chains
·
Monomers are the smaller units from which larger molecules are made
·
Polymers are molecules made from a
large number of monomers joined together in a chain
The three
major classes
biological molecules are : The
process of
·
of
monomers bonding
>
Carbohydrates with
units to
many reiseating
s
>
Lipids polymers called
>Proteins polymerisation
Carbohydrates
·
Carbohydrates are
biological molecules
important as an
energy source in cells
It
· is made up
of Carbon , hydrogen and
oxygen
atoms
>
They can be
represented by the
formula (xCH2dy
·
There are three main
types of Carbohydrates :
> Monosaccharide
>Disaccharide
>
Polysaccharide
Monosaccharides
They are
·
simple sugars
> There is one
oxygen and two
hydrogen atoms for each Carbon atom in the molecule
The [CHedn
general formula
·
is
·
Triose
Sugars (n
=
3) have 3 Carbon atoms (C3HsO3)
> breaks down triose
They are
important in mitochondria where
respiration glucose into
sugars
·
Pentose Sugars (n=ct have 5 carbon atoms (C3H100s)
>Examples are ribose and deoxyribose which are important in nucletic acids DNA and RNA
, ·
Hexose (n=6) have [C6H1202)
Sugars six carbon atoms S
> Includes
glucose , galactose and fructose
-Glucose has two isomers
they differ in only the location of
> the Hand to carbon 1
I
-glucose OH attached
groups
>A glucose has the H above carbon and the OH below
group
B-glucose
1
,
B glucose has this reversed
Disaccharides
·
Disaccharides consist two monosaccharides joined together , their is
quick-source of energy
of purpose
Two monosaccharides condensation to disaccharide
join in reaction
form molecule
-
a and
a , a
of
water is released
The bond called bond
formed between the monosaccharides is a
glycosidic
>Numbers are used to show which carbon atoms are involved in the bond
·
Three common disaccharides are
> maltose
glucose +
glucose
lactose
>
glucose +
galactose
>Sucrose
glucose fructose
+
Polysaccharides
·
Formed
by the bond of many monosaccharides joined by glycosidic bonds in a condensation run
Its and
primary functions to structure
·
are for energy storage give
They create
very compact molecules which take little
·
,
up space
·
Polysaccharides are
physically and
chemically inactive
do
s o
they not interfere with the other functions of the cell
Examples polysaccharides are
·
:
of
> cellulose
-Starch
>glycogen
is
·
Starch
important as an
energy store in
plants
It be broken
- can
rapidly down to release
glucose when needed
unbranched between
Amylose is an
polymer of 200 - 500 units
of glucose
·
have bond
They a 1-y
glycosidic
-Amylopeptin branched that be broken down to release needed
is a
polymer can
energy when
>Both 1,4 and 1
,
6
glycosidic bonds are
present
Glycogen is
important in
animals/fung
·
:
an
energy storage
>they have them
many glucose units
making very compact
have bonds
> more 1,6
glycosidic
, Lipids
Lipids which contain
hydrogen and atoms (lower (2)
macromolecules carbon
oxygen proportion of
·
are
,
Not a
polymer
·
They are non
polar and
hydrophobic
·
When oxidised their bonds broken S' Had
lipids during respiration are to release CO2
·
are
,
The
·
two
important groups of lipids are :
> Fats
> Oils
Fats animals
are
mostly from
-
solid
They are at room
temperature
-
oils are
mostly from plants
They are
liquids at room
temperature
Fats and oils made triglycerides
mainly of
·
are
up
·
A
triglyceride consists
of a molecule
of glycerol with three
fatty acios attached
25H803
Glycerol
carbony
Hydro-200H group
Fatty acid >
ester
bond
condensation/
-e-
n - - on or
*
R
esterification
H
di o -C
s
R
!
I
- -
-
0H Or -e R I
iP
H - -
H -p
&H OH e R
hydrolysis - 0 -
e - R
H 2
- - -
-
I H -
e -
- -
R
I
3 H
glycerol fatty
acids t
riglyceride
fatty acids and
glycerol combined bonds
·
are with ester
The bond
formed in condensation reaction between the
carboxyl fatty acid
-
is a
group of a
and one of the
hydroxyl groups from each acid
-A molecule of water is removed the bond created is called an ester bund
-This condensation reaction is called esterification
Triglucerides lipids that store
·
are
energy
Phospholipids are
lipids that form membranes
·
Test emulsion add to ethand and
lipids test mix add water
-
for are : -
,
to
-milky white
droplets formation indicates
positive
, Proteins
Proteins are macromolecules and are
important in nutrition
-Proteins have a
variety of roles
including :
needed
>Making enzymes for metabolism
>Make hormones
up
>Make antibodies
Amino blocks
acids the
building proteins
·
are
of
condensation
They together in
-
join reactions
The
general formula Amino acid :
for
-
does not
in
*
R &
>Amino acids contain amine
groups
(-NH2),
participate ran
2"
I
H-N-e
-
OH
Carboxylic acid (-COOH)
groups and
-
a
between
may vary
H carboxyl Side chain which is shown as
[
amino acids
Amino
group
group
Bonding in Proteins
Peptide bonds
The bonds in between acids called bonds
amino
peptide
·
proteins are
·
A
dipeptide bond is
formed when 2 amino acids are involved
bond acids involved
A
polypeptide is when
many amino
·
are
-OH
R O
↑ 11
H
N-
H -
-
-
+ - -
I
R
R P
I e-
H-N - e- C
- - -
N -
e -0H +
H20
I A
i H it it
Peptide
bond
-
Peptide bonds are
strong
Disulfide Bond
Occurs acids that the
only in Certain amino
cysteine
·
is
> The amino acid should contain a
sulfhydryl /-SH)
group
The 3H linked dithol by oxidation
groups are
covalently as a
Disulphide bonds be
formed between different chains ofamino acids between different
-
or
may
the chain
parts of .
, It provides some
rigidity to the molecule
-
protein
Hydrogen bund
·
This is formed between a
hydrogen bond and an
electronegative atom like
oxygen nitrogen ...
-It the between
is
electromagnetic attractive interaction
polar molecules ,
in which
hydrogen is
bound to a
highly electronegative atom
Amino acids with Side chains
containing -NHz in
H-bonding
·
OH etc
participate
-
..
,
-
It is a weak bond
O
21
N-2 -
C -
in
e -
H -
0
H
C
H
H 0
"Ange
H
St
trugen
bond
-
-
-
-
Ionic bund
formed between acids
oppositely charged amino
·
>Van der Wals force is a transient ,
weak electrical attraction
of one atom to another
-
CH2-CH2-CH2 -NHS -
↑
-
O-8-etz-
Tonic
bond
Hydrophobic bond
Created between two
polar groups hydrophobic amino acids
·
non or
-forms interior hydrophobic protein side chains
an , core ,
where most
hydrophobic can
closely associates
Sheilded
are
from interactions with Solvent water
CH
/
HyC CH3
H32 CH3
-
I
CH
, Protein Structures
Primary Structure (i)
·
Based the the amino acids found the
on
sequence of in
proteins
and
3 The
Sequence determines the
shape function of the
protein
(i)
Secondary structure
The localised
shape protein
·
of a
secondary structures can either be:
X-helix-formed due between
> to
hydrogen bonds
forming the
Oxygen of the -co
group
of one amino acid and the
hydrogen of the -NH
group of the amino acid
four
p
laces ahead of it (every fourth pepticle bond)
This
folding
-
causes a
>B-pleated sheet -
a looser
shape from an & helix
this occurs when the
hydrogen bonds are not
strong enough to
form an a-helix
Tertiary Structure (3)
The three-dimensional
which
protein coils to form shape
·
in
way a a
percise
-Four bonds are
responsible for maintaining their
tertiary structures :
>Hydrogen bonds Ionic bonds
>
Disulfide bonds bonds
>
>Hydrophobic
Quaternary Structure (ii)
When
·
two chains associated
or more
polypeptide join together or are with each other
The chains held bonds
together by the for tertiary
are also same structures
Types of Proteins
Fibrous
proteins
like
-Strand
shape
Typically multiple ,
Strands join to
form a
fibrous protein
covalent bunds and
disulfide bridges are
found in them
-
Hydrogen bonds are also
present
-
Examples of fibrous proteins
:
-
>Collagen
> Keratin
> elastin
-
Insoluble in water
, bones
-
found in connective tissue ,
tendons and
to
contains little no
tertiary structures
Globular
protein
·
Has a
Spherical shape
·
Hydrophillic amino acids are
found on the exterior of the
shphere
-Enables the to
protein interact water
with
Hydrophobic amino acids
found the interior
·
are in
soluble water
-
in
-Examples of globular proteins
> Plasma
proteins
>
Enzymes
>
Haemoglobin
to
Contains tertiary quaternary structures ,
allowing them fold into
globular shapes
-
and
cannot be
easily separated
·
Have due the
Carbonyl and Amino ends
ionic
properties to
conjugated proteins
A that combined with another molecule
protein
·
is
The other molecule attached to the called the
protein
is
prosthetic
·
group
- It can be :
>Organic
-
Carbohydrate -
Nucleic acid
Lipid
-
>
Inorganic Iron
-
Carbohydrate
+
protein Glycoprotein
Lipid
+
protein
>
Lipoprotein
Nucleic acid +
protein >Nucleoprotein
Iron+ Haemoglobin
protein
-
The (LDLs)
two
forms of lipoproteins : Low
density lipoproteins
(HDLs)
High density lipoproteins
Collagen
-
Provides
strength to
your
tendons , ligaments , bones and Skin
-Has tensile similar to steel
a
Strength
Very important structural
protein in vertebrates
formed from three
polypeptide chains held
by hydrogen bonds to
form a
triple
helix
Ctropocollagen)
, Haemoglobin
- Has a
quaternary structure
-Made two a subunits two subunits
up of and
2
B
↳
&
⑳
->
2
Fe prosthetic
+
group
connected by bond
a
disulphide
-Both a
globular protein and
conjugated protein
Chaem)
Each
polypeptide chain
surrounds an iron
containing group
-
