Biomolecules: A. Synthesis & Hydrolysis Reaction Vocab

Biomolecules
8/1/07
Cell Biology 1 Biomolecules
A. Synthesis & Hydrolysis reaction

Vocab:
monomer
mono = one
meros = piece/part

polymer
poly = many
meros = piece/part

Synthesis = to make/build

Hydrolysis
Hydro = water
lyse = to break

1. Synthesis reaction
(Condensation reaction, Dehydration synthesis)

- In such a reaction a H atom is removed from the
end of one building-block molecule and a
hydroxyl (OH) group from the end of a second
molecule. The two molecules are now joined
together (polymerization) i.e.,

H-A-OH + H-B-OH ! H-A-B-OH + HOH
C
6
H
12
O
6
+ C
6
H
12
O
6
! C
12
H
22
O
11
+ H
2
O

- Analogy: shifting of boxcars on a train, where
H(engine) + A (a boxcar) + B ( another boxcar)
+ OH (caboose)

2. Hydrolysis reaction
- Synthesis reactions are reversible; the complex
organic molecules can be hydrolyzed into
simpler building-block molecules

H-A-OH + H-B-OH " H-A-B-OH + HOH

Notes
Monomers are linked to other monomers by
covalent bonds to form polymers.
Biomolecules

B. Carbohydrates
sugars, starch, and cellulose being typical
representatives

Energy source

Compounds composed of carbon, hydrogen, and
oxygen, (C, O, H)
- with the empirical formula of C
n
H
2n
O
n

-
the molecular formula may also be expressed as
C
x
(H
2
O)
y

- in simple sugars x=y
- in complex sugars y=x-(n-1) where n=number of
monomer units

1. Monomer: Monosaccharides (Simple sugars)
- are the simplest sugars (generically referred to as
glucose)
- serve as building blocks for more complex
sugars

- named and classified on the basis of the length of
their carbon chain
e.g., 5-C sugars are pentoses, 6-C sugars are
hexoses
- these sugars may have other names, but generally
end in oses.

Three most common sugars utilized by cells for
energy and structural purposes are the hexoses;

glucose, fructose, and galactose (aka glactose).
Healthy Eating
Daily intake ratio of:

Carbohydrate (sugars) = 70-65% (<60%)
[fibre 20-30g] GI less than 55; GL less than
10.

Lipids (fats) = 20% (25-40% ) and (<10%
from saturated fats, 5%) (ave. intake in US
= 37%)

Protein = 12-15% (0.8 g per kg ave., 1.2-
1.6 per kg active, max 1.8)

Water = 1 L per 1,000 kcal of food eaten
plus...

A tenet of a good diet is to vary your diet,
eat bright coloured fruits and vegetables,
more raw F & V, and at least 5 servings of F
& V a day. Eat well and exercise.

Calories
To calculate your caloric needs,
Activity Level - Calories (kcal/kg)

Inactive 27
Lightly active 30-34
Moderately active 36-45
Very active 47-56
Intensely active 56-68+

Your body weight (kg) x level of activity
e.g., 70 kg x 50 (very active) = 3,500 kcal
per day

% kcal from carbs 3500 x 65% = 2275 kcal

carbs have 4 kcal/g, 2275 kcal / 4 = 568 g of
carbs a day (or about 6 - 8 g of carbs per kg
of body weight a day)
Biomolecules

Source: http://users.rcn.com/jkimball.ma.ultranet/BiologyPages/C/Carbohydrates.html

NB. Glucose, fructose, and galactose have the
same chemical composition, but different
chemical properties; they are isomers. (Galactose
differs in only single hydroxyl group so it is an
epimer, an isomer that differs only in the
configuration at a single atom.)
- glucose is formed in green plants by
photosynthesis i.e.,

6CO
2
+ 6H
2
O + Light energy ! C
6
H
12
O
6
+ 6O
2

- It is the pentose sugars (ribose and deoxyribose)
which are of critical importance as structural
elements in the formation of nucleic acids, i.e., DNA
and RNA

Monosaccharides are the "small building blocks"
used to form large molecules.

2. Disaccharides (still a relatively simple sugar)
- consist of two such molecules linked (via a
synthesis reaction) together:

Mono + Mono = Di + Water
glucose + glucose = maltose + water
glucose + fructose = sucrose + water
glucose + galactose = lactose + water

- the above reactions are reversible (hydrolysis)
- sugar molecules are transported within the body as transport disaccharides

Biomolecules
- In Lactose the bond formed between the two monosaccharides is called a beta
glycosidic bond (figure). The alpha glycosidic bond, found in sucrose and maltose, differs
from the beta glycosidic bond only in the angle of formation between the two sugars.
Unfortunately, unlike alpha glycosidic bond, beta-glycosidic bonds are unable to be
digested by some people. Therefore, many people are lactose intolerant and suffer from
intestinal cramping and bloating due to the incomplete digestion of the substance.

3. Polysaccharides (complex sugars)
- are long-chain molecules made up of repeated
monosaccharides
- Starch and cellulose are common plant examples
- Glycogen is typical of animals

a. Cellulose is the most prevalent polysaccharide on
Earth, with at least 50% of all of the carbon in
plants in this form. (structural support)
- e.g., purest state: cotton & linen
- structure is unbranched

b. Starch is a plant reserve carbohydrate (storage form
of glucose)
- structure is branched

c. Glycogen is stored in the liver and muscle cells, like
starch, is a reserve carbohydrate which can be
drawn upon when energy needs demand.
- structure is highly branched

C. Lipids
Include neutral fats, oils, waxes, and steroids (etc.)

Glycemic Index (GI)
Refers to how quickly a complex sugar
can become a simple sugar this can
elevate insulin levels rapidly which is not
good for diabetics, or your immune
system
- Banana, under-ripe 42
- Banana, ripe 54
- Banana, over-ripe 64

- Glucose 100
- Sucrose 65
- Lactose 49
- Fructose 25

- White bread 71

- Processed foods tend to have a
higher GI, while fruits and
vegetables (especially uncooked),
whole grains have a lower GI.

- Odder yet GI often varies from
country to country, US cereals
tend to have a higher GI than
Canadian cereals of the same
brand.

- Australia requires food to be
labeled for its GI
- http://www.glycemicindex.com/
Carbohydrates that contain more than two
simple sugars are called oligosaccharides or
polysaccharides, depending upon the length
of the structure. Oligosaccharides usually
have between three and ten sugar units while
polysaccharides can have more than three
thousand units. These large structures are
responsible for the storage of glucose and
other sugars in plants and animals.
Biomolecules
Fcn:
(1) as structural component of membranes.

(2) as storage forms of metabolic fuel e.g. fats.

(3) as transport forms of metabolic fuel e.g. fatty
acids.

(4) as protection against shock and insulation agents
in cells/tissues.

Organic compounds; C, O, H

All are insoluble in water (hydrophobic),
- but are soluble in oil and non-polar substances

WHY?
- The C-H bond of fats is nonpolar and cannot form H
bonds. Because of the large number of C-H bonds
that they contain, fat molecules are hydrophobically
excluded by water, since water molecules seek to
form H bonds with other water molecules. The result
is that fat molecules cluster together and are therefore
insoluble in water.

Many more C-H bonds than carbohydrates, as such able
to store more Energy

Fats are composite molecules, each made up of two
sub-units:
e.g.,
Neutral fat / triglyceride = 1 glycerol + 3 fatty acids

i. Glycerol (head)
- a 3-carbon alcohol, each of whose carbons bears a
Head Tails
Glycemic Load
You might have second thoughts about eating
a carrot with a GI of 92, vs. a carrot muffin
with a GI of 62.

Common sense tells you that a carrot ought to
be good for you. Thats where Glycemic Load
(GL) comes in: it takes into consideration a
foods Glycemic Index as well as the amount
of carbohydrates per serving.

A carrot has only four grams of carbohydrate,
per 80 g servings. To get 50 grams, youd
have to eat about a 3/4 of a Kg of them, that
carrot muffin has 28g per 60 g serving, so just
two muffins will do it. GL for a carrot is 4,
for the muffin 17.

GI of 55 is low; GL of 10 is low.

A GI is 70 or more is high, a GI is 56 to 69
inclusive is medium, and a GI of 55 or less is
low.

A GL of 20 or more is high, a GL of 11 to 19
inclusive is medium, and a GL of 10 or less is
low.
Biomolecules

Saturated fats Unsaturated fats

Source

Animal, tropical oils

Vegetable, fish oils

Examples

Beef fat, butter, palm, coconut

Canola (Canadian Oil), olive, peanut

State

Solid or semi-solid

Oil

Defined
(diagram)

Saturated with, i.e., contains only C-
H bonds (excluding functional group
carboxyl)

Not saturated with just C-H, also has
at least 1 C=C (monounsaturated), or
many C=C (polyunsaturated)
hydroxyl group
- the 3 Cs form the backbone of the fat molecule, to
which 3 fatty acids are joined

ii. Fatty acids (tails)
- important building blocks of lipids

- long hydrocarbon chain ending in a carboxyl group
(COOH)
- Includes both saturated and unsaturated fats

Fatty acids are the building blocks of fats.
Some fatty acids are "essential" because we need
them to live, yet we cannot manufacture our
own, so we must ingest them through the foods
we eat. The word "essential" is used to mean
"must be ingested". Other fatty acids are
manufactured by the body, thus although we
need them, they are not labeled as "essential".

The polyunsaturated fatty acids -- chemically
speaking, those that are not "saturated" and thus
have more than 1 double bond -- are divided into
families depending on where their end-most
double bond is located. There are two main
subtypes of fatty acids: the omega-3 and omega-
6 fatty acids. The Omega-3's are those with their
endmost double bond 3 carbons from their
methyl end. The Omega-6's are those with their
endmost double bond 6 carbons from their
methyl end.

Linoleic acid (an omega-6) and alpha-linolenic
acid (an omega-3) are the only true "essential"
fatty acids, because although a slow process,
given enough alpha-linolenic acid, the body can
synthesize eicosapentaenoic acid (EPA) and
docosahexaenoic acid (DHA) -- both important
fatty acids of the omega-3 family. But, in order
to effectively increase the body's stores, they too
must be consumed.
Biomolecules
Energy

More C-H, therefore more E per gram
(~ 9Kcal)

Fewer C-H, because of C=C,
therefore less E

Health

Excess associated with Heart Disease,
e.g., Arteriosclerosis

Essential fatty acids, essential for
good health.

Can be Hydrogenated (trans fatty
acids), associated with Cancer, Type
2 diabetes, and Heart Disease.

Energy Storage
- fats are very efficient because of the high concentration of C-H bonds
- most fats contain over 40 C atoms
- the ratio of C-H bonds to C atoms is more than twice that of carbohydrates

Fats yield Carbohydrates yield
9 kcal of chemical energy per gram 4 kcal of chemical energy per gram

- the more highly saturated the fat, the more energy, the
more calories
- animal fats are more saturated

- BUT large amounts of saturated fats upset the normal
balance of fatty acids in the body, which may lead to
heart disease
- humans are not carnivores, but omnivores
- traditionally most of dietary needs have been met by
plants, not meat

- the total amount of carbohydrates consumed is handled
in three ways:
1) held as glucose for immediate use
2) converted to transport disaccharides, for shipping
3) converted to glycogen and then fats for future use

- the reason people gain weight as they grow older is that
the amount of carbohydrates decreases, but food intake
does not. More carbohydrates are then available to be
converted to fat

Good & Bad

Low Density Lipoproteins: LDLs transport
cholesterols from the liver to cell membranes,
excess can cause arteriosclerosis (hardening of
the arteries).

High Density Lipoproteins: HDLs scavenge
excess cholesterols, to prevent hardening of
the arteries.

Note there are many types of LDL and HDLs,
some are better at their job than others.
Bigger, fluffier HDLs scavenge much more
cholesterola simple blood test for LDL and
HDL levels would not tell you what kind you
have
Biomolecules

Polymers

1. Triglycerides
- aka Neutral fats
- animal fat

2. Phosopholipids
- The basic foundation of the cell membranes is a lipid
bilayer, formed of a double layer of phospholipids

- is amphiphatic, both hydrophobic and hydrophilic
- in which the nonpolar hydrophobic tails of the
phospholipids molecule point inward, forming a non
polar zone in the interior of the bilayer .

- Lipid bilayer membranes are permeable to oxygen, to
lipids, and to small uncharged molecules, and water;

- they are not permeable to large molecules if they are
polar, or to anything that is charged, such as ions and
proteins.

- the flow of such material into and out of the cell is
Water is permeable because of aquaporins,
the molecular [protein] aqueducts that
transport water in and out of cell membranes.

Yes, proteins are chargedreview your notes
on buffers and proteins.

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Biomolecules
controlled through special protein gateways embedded
within the bilayer (facilitated / active transport) or by
bulk transport (endocytosis and exocytosis)

(NB. We will discuss this further when talk about the
fluid mosaic model a two-dimensional fluid of
freely diffusing lipids, dotted or embedded with a
mosaic of proteins.)

Note the difference between Carrier proteins and Channel
proteins

Source:
http://commons.wikimedia.org/wiki/Image:Facilitated_diffusion_in_cell
_membrane.svg

- Lungs are a collection of a huge number of small
bubbles called alveoli, which provide about 100
square metres of surface area for exchange of gases.
To allow exchange of gases the walls of the alveoli
must be very very thin, and as such the walls are not
strong enough to maintain their bubble shape against
the strong force of surface tension created by water,
(about 0.07 N/m), causing the bubble to collapse.

- The body overcomes the problem by reducing the
Glycolipids (gl)
- are carbohydrate-attached lipids.
Their role is to provide energy and
also serve as markers for cellular
recognition.
- also to attach cells to form tissues

Glycoproteins (gp)
- a group of extracellular protein-
carbohydrate compounds, e.g.,
- mucins (mucous), protective coating
holding in moisture, and preventing
proteolysis (digestion by proteases),
e.g, in the stomach
- are important for immune cell
recognition
o antibodies (immunoglobins)
o major histocompatibility
complex (or MHC)
- bind tissues
- also include hormones such as,
o Human Chorionic
Gonadotropin
o Follicle stimulating hormone
o Luteinizing hormone
o Thyroid stimulating hormone

Lipoproteins (lp)
- a combination of fat (cholesterol) and
protein that transports lipids, such as
cholesterol,in the blood.
- HDL (high density lipoprotein),
the good cholesterols
- LDL (ow density lipoprotein), the
bad cholesterols

Carrier/Channel Protein (cp)
- an integral protein that acts as a
gateway for water, Na
+
and the like
o e.g., aquaporins, Na
+
/ K
+

pump, glucose carrier
- Carrier Protein - an integral
membrane proteins that bind to a
"substrate" and transport it across the
membrane
o aka Carrier Molecule
- Channel Protein - an integral
membrane protein that acts as pore

Biomolecules
surface tension of water by secreting the

- phosopholipid (called di-palmitoylphosphatidyl
choline (DPPC)) to act as a detergent or surfactant.

- Surface tension arises from the hydrogen bonding
between water molecules, which holds the water
molecules together e.g. in a water droplet like a large
crowd holding arms together. The DPPC fits in
between the water molecules so disrupting the
cohesive hydrogen bonds reducing the surface
tension like policemen going into a crowd and
breaking up the arm holding. In the presence of
DPPC the surface tension is reduced to a very low
level of 0.01 N/m.

- Notice that there are molecules of cholesterol
(lipoproteins) embedded in the membrane.
Cholesterol is a necessary component of biological
membranes. Cholesterol breaks up the Van der
Waals interactions and close packing of the
phospholipid tails. This disruption makes the
membrane more fluid.

3. Steroids
- A substantially different group of lipids from those
already considered examples are cholesterol,
oestrogens, androgens, progesterone, bile salts and
are characterised by having ring structures.
- composed of four carbon chains, resembling
chicken wire
- structurally they are different from other lipids, but
are "soluble in nonpolar organic solvents" (i.e.,
oils)

Cholesterol is:
- an important structural component of cell membranes

- precursor of steroids in animals, especially of male and
female sex hormones

Biomolecules
- manufactured by plants but vital to animals because of
their involvement in the chemistry of vision, and
vitamins such as A, D, E, and K; e.g., carotene

4. Prostaglandins
- are a group of 20 lipids that are modified fatty acids
(phospholipids), with two nonpolar tails attached
to a five carbon ring.

- occur in vertebrate tissue, where they appear to act
as local chemical messengers
- some stimulate smooth muscle (e.g., uterus) to
contract or expand the diameter of small blood
vessels

- In women
- (Type E2 and F2 alpha) stimulate uterine
contractions when a woman goes into labour,
and which are recognized as cramps during the
menstrual period,
- a surge in lutenizing hormone (LH) promotes
the intrafollicular production of
prostaglandins A and E, which are associated
with rupture of the follicle; ovulation
- is also key in the demise of the corpus luteum
(and subsequent decrease in progesterone
levels)

- In males
- (Type E1) is a vasodilating agent which acts by
relaxing the smooth muscles of the corpus
cavernosum and by increasing the diameter of
cavernous arteries; this leads to erection.
- male seminal fluid is rich in prostaglandins that
increases sperm motility and viability,
decrease mucous viscosity at cervix, and
stimulate female uterine contractions to move
the semen up into the uterus (may be acting as
a pheromone)

More About Prostaglandins
There are many different types of prostaglandins,
all of which affect muscle tension. However, not all
prostaglandins affect muscles in the same way.
Some, such as the series two prostaglandins
(specifically the E2 and F2 Alpha), trigger powerful
smooth muscle contractions. Because of this
physiological effect, an overabundance of series two
prostaglandins is strongly linked to menstrual
cramps and pain. These prostaglandins have also
been linked to high blood pressure because they act
to narrow the diameter of blood vessels. They can
also trigger irritable bowel syndrome since they
cause cramping of the intestinal muscles. Not all
prostaglandins, however, cause muscle contraction.
Others, such as the series-one and series three,
actually promote muscle relaxation and can help
relieve menstrual cramps.

Prostaglandins are derived from fatty acids in the
diet. The series two prostaglandins that trigger
muscle contractions are derived from animal fat
meat, dairy products, and eggs. The beneficial
muscle relaxant series one and series three
prostaglandins are derived from vegetable and fish
sources of fatty acids. These fatty acids, called
linoleic acid and linolenic acid, are found
predominately in raw seeds and nuts, such as flax
seed or pumpkin seed, and in certain fish, such as
trout, mackerel, and salmon. Thus, how we eat can
actually determine which hormonal pathway we
travel, leading to either muscle tension or muscle
relaxation. This is a very good example of how
our food selection can determine our state of
health. Like progesterone, excessive prostaglandin
production is seen only during ovulatory menstrual
cycles. Prostaglandin production increases during
the second half of the cycle, peaking toward the end
of the cycle with the onset of menstruation.

Source: Susan M. Lark M.D., http://www.healthy.net
Uterine cramping is one of the most common
uncomfortable sensations women may have
during menstruation. There are two kinds of
cramping. Spasmodic cramping is probably
caused by prostaglandins, chemicals that
affect muscle tension. Some prostaglandins
cause relaxation, and some cause constriction.
A diet high in linoleic and liblenic acids,
found in vegetables and fish, increases the
prostaglandins for aiding muscle relaxation

Source: http://www.fwhc.org/health/moon.htm
Biomolecules
- involved in varied aspects of reproduction (much of
which is still unclear), and in the inflammatory
response to infection

- it is because aspirin inhibits prostaglandins
production that it reduces pain, inflammation, and
fever

D. Protein
Structural and enzymatic function

composed of C, H, O, N, and sometimes P and S

are associated with every structure in the cell and are
involved in almost every cellular activity

predominant kind of molecule found in cell
-~50% of the dry weight of living matter is protein

generally quite large

despite their diverse function, all have the same basic
structure: a long polymer chain of amino acid subunits
linked end to end

Components of :
1. Amino acids
- the building blocks of proteins
- while there are many a.a. in nature, only 20 are used
in proteins

a. General Structure:
- amino group (NH
2
); a carboxyl Acid group
(COOH); and a H atom, all bonded to a central C
atom
C
H
R
C
O
OH
H N
2

- the identity and unique chemical properties of
each a.a. are determined by the R group

2. Polypetides (the glue that binds a.a.)
-The a.a. are bonded to form a protein by synthesis
Essential Amino acids (human), must be
eaten/ingested. Most animal products, such
as meat and dairy products, contain all of
the essential amino acids and have been
designated as containing complete proteins.
Most proteins from vegetables also contain
all 9 essential amino acids, but 1 or 2 may
be low in a particular food compared with a
protein from most animal sources. Beans,
however, are rich sources of all essential
amino acids:
tryptophan,
methionine,
valine,
threonine,
phenyalanine,
leucine,
lycine
Biomolecules
between the amino group of one amino acid and the
carboxyl group of another.
- The resulting bond is a peptide bond (a covalent
bond) and the chains produced are polypeptide
chains.
- Dipeptide = a.a. a.a.
R
R R
peptide bond
a.a.
amino group
carboxyl group

- Simple Proteins:
- consist simply of a.a., e.g., Lactoglobin, C
1864

H
3012
O
576
N
468
S
21

- Conjugated Proteins:
- a.a. plus some other component, e.g., iron in
Haemoglobin, C
3032
H
4816
O
872
N
780
S
8
Fe
4

Structures:
1. Primary Structure (1)
Shape: Linear
- a linear sequence of a.a. that makes up a particular
polypeptide chain

- the R group plays no role in the peptide backbone of
proteins, as such a protein can be composed of any
sequence of a.a.
- a protein of 100 a.a. linked together in a chain
might have 20
100
different a.a. sequence
- it is this key property of diversity that allows for
such a wide range of proteins
R Radical Groups
It is these Side Groups which make each
amino acid different from the others. Of the
20 used to make proteins, there are three
groups. The three groups are IONIC,
POLAR and NON-POLAR . These names
refer to the way the side groups interact
with the environment. Polar amino acids
like to adjust themselves in a certain
direction. Non-polar amino acids don't
really care what's going on around them.
And Ionic amino acids, act much like ionic
compounds.

Tryptophan (nonpolar)
Threonine (polar)
Lycine (ionic)

Biomolecules

2. Secondary Structure (2)
Shape: Helix (alpha-helix and beta-pleated sheet)
- each a.a. of a chain interacts with its neighbours,
forming H-bonds
- because of these interactions, polypeptide chains
tend to fold spontaneously into sheets or wrap into
coils
- this change in shape is called its secondary
structure

3. Tertiary Structure (3)
Shape: Globular (cupped hand shaped)
- a.a. in a chain also interact with water, forming a
folded helix,
- disulphide (SS) bonds often stabilise the fold.
- aka disulphide bridge
- a covalent bond formed in RER

- the nonpolar side of the chain tends to fold so that
(hydrophobic groups) are shielded from the
surrounding water
- the polar side (hydrophilic) will tend to expose
itself to the surrounding water
- all this minimizes disruption of H-bonds

- this folding leads to a complicated globular

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Priamary (linear)

Secondary

Tertiary & Quaternary
Biomolecules
shape, indicative of tertiary structure

4. Quaternary Structures (4)
- results when two or more Polypetides unite to
form a multimeric protein
- proteins with more than one polypeptide chain
are said to be oligomeric

- e.g., haemoglobin - a tetramer, containing 2
alpha + 2 beta sub-units.

Aside:
- What is the advantage of association rather than
staying as monomers? In some proteins the
subunit alone is not active - so biological activity
depends on intact oligomeric structure. So in this
case oligomeric structure provides increased
stability such that in the absence of oligomeric
structure, the single subunits are unstable.
- However, in other oligomeric proteins the
single subunit is biologically active, and
appears to act independently of the
oligomeric structure. So stability is not the
only factor involved.

- Another advantage of multiple subunits is greater
Biomolecules
flexibility of activity e.g. hemoglobin (Hb) and
many enzymes show cooperativity. In the case of
tetrameric Hb one subunit binds oxygen then
stimulates neighbour subunits to bind oxygen
more readily and so on through the 4 subunits so
the subunits cooperate to ensure rapid and
effective binding of oxygen.
- If there were no cooperativity then it is likely
that competition between the subunits for
binding oxygen would be overall less
efficient. Cooperativity is mediated through
intersubunit contacts.

- Also subunits provide an advantage in regulation
of protein activity. In proteins and enzymes
containing identical subunits it is found that the
subunits contain special sites called allosteric
sites located away from the active site of the
enzyme or protein.
- Allosteric sites bind small molecules such as
sugars, nucleotides etc., and these cause
intersubunit changes in shape that regulate
the activity at the active site so giving a fine
control over the biological activity. Not all
enzymes or proteins have allosteric sites,
many do not e.g., lactate dehydrogenase
(LDH) is a tetramer, and has no known
mechanisms of regulation.

- Lastly there is a genetic advantage in having
oligomeric structure.
- The four protein sub-units of a tetramer will
be coded by four different genes.
- If an error occurs in DNA transcription or
RNA translation producing faulty copies
of one of the sub-units, then provided
some correct copies have been produced
elsewhere of the other three other
submits, there is not a total loss of protein
activity only a partial loss, which may be
enough for survival.
- If one gene produced one polypeptide
chain, and a mutation produced an
error in the DNA then all copies of
the subsequent protein would be
faulty. If the protein is vital then the
mutation may be fatal. So oligomeric
structures may be important in
Allosteric
- enzymes, in which a compound
combine with a site on the protein
other than the active site
o the allosteric site
- Changes that enhance activity are
referred to as allosteric activation,
o the binding of oxygen
molecules to haemoglobin
o The binding of oxygen to
one subunit induces a
conformational change in
that subunit that interacts
with the remaining active
sites to enhance their
oxygen affinity.
- while the opposite is called
allosteric inhibition.
o when 2,3-BPG (2,3-
bisphosphoglycerate)
binds to a regulatory site
on hemoglobin, the affinity
for oxygen of all subunits
decreases.
Biomolecules

survival.

- Caveat: The text describes the shape as being 3
dimensional, but then all these shapes are 3
dimensional

Denaturation
- the structure of a protein is not haphazard

- any force that disrupts the delicate balance (e.g., of
weak bonds and interactions) will denature the protein,
resulting in altered structure and hence in malfunction

- Two such forces:
1. Extremes in pH, which affect charges on different
parts of the molecule

2. Extremes of temperature, which disrupts H bonds

Proteins therefore operate within a limited range of pH
and temperature

Biomolecules
Form & Function of a Variety of Proteins:

Function Form Example Use

Structure

fibres

collagen; keratin;
fibrin

cartilage; hair & nails; blood
clot

Metabolism enzymes protease
break down proteins

sodium-potassium
pump; anion pump

excitable membranes; transport
of Cl
-
ions

Membrane
transport
channels
aquaporins
water transport through cell
membranes
Cell recognition cell surface antigens
MHC proteins;
ABO blood group
self recognition; identifies
red blood cells

Osmotic
concentration
albumin serum albumin
maintains osmotic
concentration of blood

Regulation of gene
action
repressors lac repressors
regulates transcription

Regulation of body
function
hormones
insulin; vasopressin;
oxytocin
controls blood glucose levels;
increases water retention by
kidneys; regulates milk
production

Transport
throughout the
body
globins
hemoglobin;
myoglobin;
cytochromes
carries O
2
and CO
2
in blood;
carries O
2
and CO
2
in muscle;
electron transport
Contraction muscle actin; myosin contraction of muscle fibres
Defense
immunoglobins;
toxins
antibodies; snake
venom
mark foreign proteins for
elimination; blocks nerve
function

Aside: Plasma protein refers to any protein found in the blood plasma, e.g, hemoglobin, albumin,
immunoglobins, various peptide hormones etc.

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