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BIOMACROMOLECULES

The document summarizes biomacromolecules and their properties. It discusses that the four main elements that make up life are hydrogen, oxygen, nitrogen, and carbon. It then focuses on carbon and its unique bonding properties that allow it to form large, complex organic molecules like lipids, carbohydrates, proteins, and nucleic acids. These molecules are called macromolecules and are made up of smaller repeating units called monomers that are bonded together via dehydration reactions to form polymers. The four main types of macromolecules and their monomer units are discussed in detail.

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0% found this document useful (0 votes)
225 views

BIOMACROMOLECULES

The document summarizes biomacromolecules and their properties. It discusses that the four main elements that make up life are hydrogen, oxygen, nitrogen, and carbon. It then focuses on carbon and its unique bonding properties that allow it to form large, complex organic molecules like lipids, carbohydrates, proteins, and nucleic acids. These molecules are called macromolecules and are made up of smaller repeating units called monomers that are bonded together via dehydration reactions to form polymers. The four main types of macromolecules and their monomer units are discussed in detail.

Uploaded by

Aina Mira Palou
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as DOCX, PDF, TXT or read online on Scribd
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BIOMACROMOLECULES

ELEMENTS IN HUMAN BODY

Even though there are more than 92 natural elements


found on the Earth, almost all life forms are made up only
of four basic elements: hydrogen, oxygen, nitrogen and
carbon.

Much of the cell’s content is a watery soup with small


molecules and ions. A 70-95% of the cell is water, the rest
are carbon compounds. A 95% of mass of cells are only 6
elements: C,H,O,N,P,S.

CARBON PROPERTIES

Living organisms are made up of chemicals based mostly on the element carbon (C).

Most of the molecules in living things are organic molecules, meaning that they contain carbon.
Organic compounds range from simple molecules to complex ones, with thousands of atoms
and high molecular masses.

Carbon has 4 electrons in its outermost shell, this tetravalence is the one facet of carbon’s
versality that makes large, complex molecules possible.

Carbon is capable of covalently bonding with other atoms to fill its outermost shell.

BONDING ROPERTIES OF ATOMS


HYDROCARBONS

Are carbon and hydrogen molecular skeletons. Carbon chains form the skeleton of most organic
molecules. There is a big variation in carbon skeletons that is one important source of the
molecular complexity and diversity that characterize the living matter.

FUNCTIONAL GROUPS

The functional groups are groups of


atoms acting as a unit that gives to the
organic molecules their own physical
properties. They have chemical
reactivity and solubility in aqueous
solutions.

THE ORGANIC MACROMOLECULES

There are four major kinds of organic molecules:


- Lipids
- Carbohydrates (glucids)
- Proteins
- Nucleic acids

These molecules are often called macromolecules because they may be very large, containing
thousands of carbon and hydrogen atoms and because they are typically composed of many
smaller molecules bonded together.

The base elements of carbohydrates and lipids are Carbon (C), Hydrogen (H) and Oxygen (O).
Protein is also made up of these base elements but it also contains Nitrogen (N).
When viewing the chemical structures of carbohydrates, lipids and proteins you can distinguish
proteins from the other two by the presence of N in its chemical structure.
The large molecules are chain-like molecules called polymers. A polymer is a long molecule
consisting of many similar o identical building blocks (monomer)linked by covalent bonds. The
repeating units of polymers are small molecules called monomers that are covalently bonded
together to create a large polymer molecule.

 The monomer unit for carbohydrates is a monosaccharide. When two of these


monosaccharides are linked by covalent bonds a disaccharide is created. When several
monosaccharides are bonded together a polysaccharide is created.

 Proteins are made up of monomers called amino acids. There are twenty amino acids
and they can be strung together in unique combinations known as polypeptide chains,
the polymer unit for proteins. A protein is only complete and functional when the
polypeptide chain is folded into a unique 3-D shape.

 Nucleic acids are made of nucleotides. There are four different nucleotides for DNA –
A,C,T,G, and RNA – A,C,U,G.

 The exception to the monomer/polymer rule are lipids. Lipid base units are not
considered monomers. One type of lipid is made up of fatty acids and glycerol
molecules in a 3:1 ratio. The bonding of three fatty acids to one glycerol molecule
creates a triglycerides = fats or oils.

Monomers are joined together by condensation


(dehydration) reactions, which form water
molecules in the process. Polymers can also be
broken into monomers by hydrolysis reactions,
which use water molecules in the process.

Monomers, or base units are bonded together to


create larger molecules via dehydration. This
involves the removal of a water molecule at the
bonding site. The larger molecule can be broken
down by the reverse process, hydrolysis. This
occurs when water is added to break the covalent
bonds created during dehydration.

In biological systems, macromolecules are often


formed by removing -H from one atom and -OH
from the other. The H + OH combine to form
water. Small molecules (monomers) are
therefore joined to build macromolecules by the
removal of water (dehydration = condensation).

 Condensation Reactions: involve release of water H2O, joining together of two


monomers by covalent bond to form polymer. Occurs in biosynthesis.
General formula: A-OH + H-B A-B + H2O
 Hydrolysis reactions: reverse of condensation. Involves adding water to split covalent
bond, release of two smaller molecules. Occurs in digestion.
General formula: A-B + H2O A-OH + H-B

Organic molecules with the same chemical formula may have different molecular structures. For
example, C6H12O6 is the formula for fructose, glucose, and galactose. All three are simple sugars,
but because of differences in structure they differ in their chemical properties. Molecules
related in this way are called isomers.

ISOMERS

There are four types of isomers:

 Structural: have the same empirical formula but different structure.


 Geometric (cis/trans): differ in arrangement of groups attached to C=C.
 Optical: bend plane of light in different directions (mirror images).
 Enantiomers: are isomers with identical chemical properties but its rotate lane of
polarized light is located at different angles.

o Levorotatory (left handed)


o Dextrorotatory (right handed)

Enantiomers are molecules that have opposite spatial configuration and are said to be
optically active. One enantiomer will rotate polarized light a set number of degrees to
the right. This is called the dextrorotatory isomer or (+) isomer (clockwise rotation).

The other enantiomer will rotate the plane of polarized light the same number of set
degrees in the opposite left direction. This isomer is said to be a levorotatory isomer
or (‐) isomer (counterclockwise rotation).

Examples:

- R-thalidomide: effective against morning sickness in pregnant women.


- S-thalidomide: teratogenic effect causes birth defects.

CARBOHYDRATES
Carbohydrates or saccharides make up most of the organic matter at Earth. In carbohydrates
every carbon atom has H-C-OH = CH2O groups, (except one Carbon atom has a carbonyl (>C=O)
group).

Scientists came up with the name because the compounds have many carbon atoms bonded to
hydroxide groups.

Chemical formula: (CH2O)n, where n = some integer (3 or greater).

The carbohydrates have extensive roles in all forms of life:


 Carbohydrates serves as energy stores, fuels and metabolic intermediates (especially
the hexoses). Presence of -OH groups on sugars decreases energy content but increases
solubility.
Glucose is the most important monosaccharide on Earth and is used in cellular
respiration and created by photosynthesis.
An important pentose as the Ribose can be found in ATP, GTP, NADH, NADPH.

 Ribose and Deoxyribose sugars form part of the structural framework of DNA and RNA.

 Polysaccharides are structural elements in the cell walls of bacteria and plants. Cellulose
is the main constituent of plant cell walls and is one of the most abundant compounds
in the biosphere.

 Carbohydrates linked to many proteins and lipids, where they do mediating interactions
among cells and interactions between cells and other elements in the cellular
environment. Carbohydrates play major roles in the working process of the immune
system, fertilization, pathogenesis, blood clotting and development.

 Important substrates for building other necessary molecules.

 Carbohydrates are molecular tags, on membrane proteins face outside of cell, used for
recognition of specific cells and molecules. Proteins with sugar tags are called
glycoproteins.

 Glycocalyx: protection against mechanical and chemical damage. Also cell-to-cell


communication (fertilization, blood clotting, inflammation) and recognition of ‘self ’
antigens (infections, transplantations, cancer cells)

MONOSACCHARIDES
Monosaccharides generally have formulas
that are some multiple of the unit CH2O.
Glucose is the most common
monosaccharide.

The molecule has a carbonyl group and


multiple hydroxyl groups. Depending on the
location of the carbonyl group, a sugar is
either an aldose with the carbonyl group at
the end of carbon or a ketose with the
carbonyl in the middle.

Another way to classify sugars is the size of


the carbon skeleton, which ranges from the
3-8 carbons.

COMMON MONOSACCHARIDES

 Glucose: is the most abundant sugar on planet Earth.


o Is the principal sugar found in human blood, carried throughout the body as a
major source of energy for the billions of cells throughout the body.
o Some cells, such as brain neurons, rely entirely on glucose as their only energy
source. Without a steady supply of glucose they cease functioning.
o Glucose is an extremely important molecule for human metabolism.
o Blood concentration (glycemia) of glucose is carefully regulated by hormones
such as insulin and glucagon.
o Many polysaccharides are built from glucose, including cellulose that makes up
plant cell walls.

 Galactose: is an important hexose, found in lactose (milk sugar) along with glucose, and
in many plant polysaccharides.
 Fructose: also called fruit sugar.
o Is an important hexose found in many fruits and vegetables.
o Fructose satisfies the "sweet tooth", tasting twice as sweet as sucrose (table
sugar), so can be used in lower amounts.
o The switch from sucrose (cane sugar) to fructose (derived from corn) by major
soft drink manufacturers caused major problems for the economies of some
developing countries whose economies were largely dependent on sugar cane).
 Ribose: comprises the backbone of RNA, is the basis of genetic transcription. Is also a
subunit of ATP, NADH and several other compounds that are critical to metabolism.
 Deoxyribose: is found in DNA.
 Xylose: is a constituent of polysaccharides in blood.

DISACCHARIDES

A disaccharide consists of two monosaccharides joined by an O-glycosidic bond that is a covalent


bond formed between two monosaccharides by a dehydration reaction.

COMMON DISSACHARIDES

 Sucrose: glucose + fructose


o Plants usually transports carbohydrates from leaves to roots in the form of
sucrose obtained from sugar cane or sugar beets. Used to be the major sugar
used for sweetening foods, soft drinks, etc.
o Sucrose can be cleaved into its component monosaccharides by the enzyme
sucrase that hydrolyze the covalent bond.
 Lactose: glucose + galactose
o Found in milk from lactating mammals only.
o Once the bond has formed it requires a special enzyme, lactase, to break this
unusual bond.
o Certain population groups are deficient in lactase, so they are unable to digest
lactose. If this happens, the person has cramps and other unpleasant symptoms
such as nausea, pain and watery diarrhea. These people are called lactose
intolerant.
 Maltose: glucose + glucose.
o Its formed by the hydrolysis of starch by enzyme called maltase and is otherwise
not found in nature.
o Found in barley, used in beer-making process, also for malted milk drinks.
o In digestion, complex carbohydrates (such as starch) are broken down to
maltose, then further broken down to produce two glucose molecules.
POLYSACCHARIDES

Polysaccharides are polymers with a few hundred to a few thousand monosaccharides joined
by glycoside linkages. The function of a polysaccharide is determined by its sugar monomers and
by the position of its glycosidic linkages.

The monomers units can be put together in many ways, as homopolysaccharides containing a
single kind of monomer or as heteropolysaccharides with two or more monomers.

The most common polysaccharides are starch, glycogen, and cellulose. All of these are polymers
of glucose. What differs among them is how the glucose molecules are bonded together. Starch
is the storage form of glucose found in plants, Glycogen is the storage form of glucose in animals
and cellulose is plant fiber, that we cannot digest because of the way the glucose molecules are
joined together.

STORAGE POLYSACCHARIDES

The storage polysaccharides are glycogen that is found in animals and the starch that is found
in plants. Both of these polymers are branched chain polymers of glucose and they have a
function as energy reserves. Are soluble and available very quickly.

 Starch: is the storage polysaccharide from plants. Is a polymer consisting entirely of


glucose monomers bonded by an o-glycosidic bonds.
The simplest form of starch is the amylose that is unbranched. The branched form of
starch is called Amylopectin.
More than half the carbohydrates ingested by humans is starch. Both, amylose and
amylopectin are rapidly hydrolyzed by -amylase, an enzyme secreted by the salivary
glands and the pancreas.
Plants store starch as granules within cellular structures called plastids, which include
chloroplasts. Synthesizing starch enables the plant to stockpile surplus glucose.
Potato tubers are grains are the major sources of starch in the human diet.

 Glycogen: is the animals storage polysaccharide and is a polymer of glucose that is like
amylopectin but more extensively branched. Branches are created by o-glycosidic
bonds.
Glycogen is an important fuel reserve for several reasons:
o Between meals, the liver breaks down glycogen to glucose in order to keep the
concentration of glucose in the blood stable. Glycogen is especially important
because glucose is virtually the only fuel used by the brain.
o The glucose from glycogen is readily mobilized and is therefore a good source
of energy for sudden. It can provide energy at the absence of oxygen and can
supply energy for the anaerobic activity.
o After meals, as glucose levels in the blood rise, it is removed from system and
stored as glycogen. The two major sites of glycogen storage are the liver and
the skeletal muscle.
o Human body stores enough glycogen to provide sugar to blood for 24-36 hours
during fasting.
o Glycogen is broken down back into glucose when the energy is needed, this
process is called glycogenolysis.
STRUCTURAL POLYSACCHARIDES

Structural polysaccharides include cellulose and chitin.

 Cellulose: is the major structural material of which plants are made and is found in plant
cell walls.
o This provides us with fiber in our diet, wood that is largely cellulose, cotton and
paper that are almost pure cellulose.
o The rings of glucose are arranged in a flip-flop manner. A cellulose molecule is
long and straight and is never branched. Also is a rigid molecule.
o In plants cell walls, cellulose has no side chains as there in starch. Parallel
cellulose molecules held together in this way are grouped into units called
microfibrils (series of stiff or elongated fibrils). These cable-like microfibrils are
strong building material for plants as well as for humans.
o Enzymes that digest starch are unable to digest cellulose because of its different
structure. In fact, most of the organisms like humans, doesn’t possess enzymes
that can digest cellulose, so it passes through the digestive tract and is
eliminated with the feces. (Digestion requires an enzyme). It is very insoluble
and takes long time to digest.
o The fiber or roughage is important in minimizing colon cancer.

 Chitin: is the second most abundant biopolymer on Earth.


o Is a polymer of glucosamine (glucose modified by addition of amino groups).
o Makes very rigid polymer, used by insects, crustaceans, and other arthropods
as exoskeleton material (like armor).

GLYCOSAMINOGLYCANS

Glycosaminoglycans (GAGs) or mucopolysaccharides are long linear (unbranched)


polysaccharides consisting of repeating disaccharide units.
The repeating unit consists of an amino sugar (N-acetylglucosamine or N-acetylgalactosamine)
along with a uronic sugar (glucuronic acid or iduronic acid) or galactose.

Classification into 4 main groups:


 Heparin/heparan sulfate: is the most widely used GAG and the most common
therapeutic carbohydrate worldwide. Used in treatments and prophylaxis of
thromboembolic disorders because of its potent anticoagulant activity.
 Chondroitin sulfate/dermatan sulfate: has essential roles in cartilage and other
connective tissues and can be used as an alternative therapeutic in cases of
osteoarthritis, and sometimes even osteoporosis.
 Keratan sulfate: is one of principal functional components in cornea (eye). Can be
employed as active ingredient in eye drops for treatment of certain visual dysfunctions.
 Hyaluronan: is an important functional component of the ECM of skin and is used in
cosmetics to soften and smooth skin, owing to its inherent regenerative and hydrating
properties.

GAGs interact with proteins in many biological systems, and as a consequence they have
numerous biological and therapeutic functions. GAGs can be considered the most exploited
carbohydrates in the pharmaceutical market.
Glycosaminoglycans are highly polar and attract water; they are therefore useful to the body as
a lubricant or as a shock absorber.
LIPIDS
Lipids are the only class of large biological molecules that does not belong to polymers. However,
they are made by linking together smaller molecules. Among the “building blocks” of lipids are
fatty acids, glycerol and phosphoric acid.

The compounds called lipids are grouped together because they have little or no affinity for
water.

Each type of lipid has a slightly different structure, but they all possess a large number of C - H
bonds which makes them a primarily non-polar group of molecules. Also, all the C-H bonds
makes them very energy-rich.

Lipids are hydrophobic that means that lipids are water insoluble biomolecules that are highly
soluble in organic solvents. But many lipids have both polar and nonpolar regions. This gives
them an amphipathic character, for example, a tendency toward both hydrophobic and
hydrophilic behavior, and accounts for their tendency to aggregate into membranous structures.
This group of molecules includes:
- Fats and oils.
- Waxes.
- Phospholipids.
- Steroids (like cholesterol).
- Some other related compounds.

Because of their molecular structure the lipids are hydrophobic („water hating“)
Consists mostly of hydrocarbons.
Functions:
- Energy storage (triacylglycerols)
- Structural components of cell membrane (phospholipids, cholesterol, glycolipids)
- Important signaling molecules (e.g. steroid hormones, prostaglandins)
- (Insultation of the body)
Vitamin A, D, E, K also belong to the group of lipids
Some light absorbing plant pigments (e.g. chlorophyll or carotenoids) also belong to the lipids.

1.3.1. Fats and Oils (Triacylglycerols)


Fat
- assembled from smaller molecules by dehydration reactions
- constructed from two kinds of smaller molecules
o glycerol
o fatty acids
- Gylcerol: alcohol with three carbons, each bearing a hydroxyl group
- Fatty acids: consist of a hydrocarbon chain attached to a carboxyl group (-COOH)
o >12 carbon atoms = nearly insoluble in aqueous solutions (because of their long
hydrophobic hydrocarbon chains)
o NO carbon-carbon double bond: saturated
o ONE carbon-carbon double bond: unsaturated
o MORE THAN ONE carbon-carbon double bond: polyunsaturated
o Linoleic acid (C18:2)
Essential fatty acids which can´t be synthesized
by mammals and must be supplied in their diet
o Linolenic acid (C18:3)
- Fat = Glycerol + three fatty acids
Ester linkage

- can be three simillar fatty acids or three different


- saturated fat = made from saturated fatty acids
o most animal fats (solid like lard and butter at room temp.) hydrocarbon chain of their
fatty acid lack double bond.
- unsaturated fator oils = made from unsaturated fatty acids
o plant and fish fats (liquid like olive oil at room temp.)

1.3.2. Phospholipids

- only 2 fatty acids attached to the glycerol


- the third hydroxyl-group (-OH) of the glycerol is attached to
a phosphate-group
- most phospholipids found in membranes
- Suspension of phospholipids is mechanically dispersed in
aqueous solution the phospholipids aggregate into one of
three forms:
o Micelles
o Liposomes
o Phospholipid bilayers

1.3.3. Steroids

- Characterized by a carbon skeleton consisting of four fused rings


- Different steroids vary in the functional groups attached to this ensemble of rings
- Cholesterol:
o Common component of animal cell membranes and is also the precursor from which
other steroids are synthesized
o Hormones (e.g. cortisol, aldosterone)
o Sex hormones (e.g. progesterone, testosterone)steroids produced from cholesterol
o Vitamin D
- Critical molecule in animals and humans
o High level ->atherosclerosis

PROTEINS
Definition: Proteins are large organic compounds made of amino acids arranged in a linear
nonbranched chain and joined together by peptide bond (is a covalent chemical bond linking
two consecutive amino acid monomers).
Proteins are trully the physical basis of life and constitute most cell’s dry mass (more than 50%).
Proteins are macromolecules, a typical protein contain 200-300 aminos acids,(the smallest are
called peptide, the largest is titin founded in skleletal and cardiac muscle, it contains 26,926
amino acids in a single chain).

Function:
- Many proteins are enzymes that cathalizes biochemical reactions and are vital to the
metabolism. Enzymes accelerates reactions by lowering the activation energy barrier.
- Structural function as colagen, elastin and keratin.
- Cell signaling serving as a receptor (eg. Receptors built into the membrane of a cell
detecting chemical signals released by other cell)
- Transport proteins involved in the transport of other substances (eg. Hemoglobin, iron-
containing protein that transports oxygen from the lungs to the body).
- Motor proteins moving parts (eg: kinestin, propels organeles through the cytoplasm).
- Atibodies – defensive proteins (imune response).
- Storage proteins, form ready resorces of amino acids.

Structure: To have a protein we need:


-20 to 21 different amino acids are used to synthisize a
protein. (polymers of amino acids are called
polypeptides.
- a hydrogen atom - an amino group ( -NH2)- a carboxyl
group (- COOH)
- one of the 20 different side chain ( “R” group)

The stucture of the “R” group determine which of the 20 it is and the properties.
Amino acids can be divide into 4 main classes according to the protperties of their side chain:
- (1) nonpolar or hydrophobic
- (2) polar or hydrophilic
- (3) polar negatively charged(acidic)
- (4) polar positively charged (basic)

We can use the 3 first letters of them to nominate it (eg. Ala, Leu, Iso, Val, etc)

Structure: Peptide bond


Dehydration reaction (condesation) between the amino group of the amino acid 1 with the
carboxyl group of the amino acid 2, releasing water.
2 amino acids joined = dipeptide
3 amino acids joined = tripeptide
4 amino acids joined = tetrapeptide
many amino acids joined = polypeptide

Polypeptide is the precursor of a protein, as assembled on the ribosome during translation, the
molecule is called polypeptide. When released from ribossome following translation, it folds up
and assumes a higher order of structure called protein.
N – terminus is the end of the polypetide chain that contains a free amino group.
A peptide bond can be broken by hydrolyisis (add water), but this process is really slow so
enzimes are used to facilitated it.

Structure:
 Primary structure: the linear arrangement of amino acids in a protein/polypeptide and
the location of covalent linkages such as disulfide bonds between amino acids.
 Secondary structure: areas of folding or coiling within a protein; examples include
alpha helices and pleated sheets, which are stabilized by hydrogen bonding.
 Tertiary structure: the final three-dimensional conformation of polypeptide, which
results from a large number of non-covalent interactions between amino acids.
Forces that contribute to a tertiary folding: stabilize the molecule of protin, determin
conformation:
o Hydrogen/ionic
bonds
o Hydophobic force
o Van der waals
atraction
o Disulphide bonds.
(-S-S – bonds). These
are speacially
important, because
they are covalent
bonds and quite
strong compared
with H- bonds.
 Quaternary structure: non-
covalent interactions that
bind multiple polypeptides
into a single, larger protein.
Hemoglobin has quaternary
structure due to association
of two alpha globin and two
beta globin polyproteins.
Protein Folding in cell is NOT only a
sponteneous process, as for many
proteins, folding is dependent upon
members of a family of still other proteins
called chaperones .

2 general families of chaperones are


recognized:
(1) Molecular chaperones: are
proteins that assist the covalent
folding or unfolding and the
assembly or disassembly of other
macromolecular structures.
(2) Chaperorins: are a class of chaperones that assist in folding of (largely) newly
synthesized proteins.

Denaturation is a process in which proteins lose the quaternary structure, tertiary


structure and secondary
structure which is present in
their native state, by
application of some external
stress or compound such as a
strong acid or base, a
concentrated inorganic salt,
an organic solvent or heating.

Renaturation is the reverse


process

NUCLEIC ACIDS
Definition: Nuclic Acids are long linear polymer formed by attaching together monomers caled
nucleotides.
Nucleotides consists of a phosphate, a 5- carbon sugar and a nitrogeneous base.
There are 4 kinds of nitrogenous bases in DNA, divide into two classes Purines and Pyrimidines.

Purines: Adenine (DNA and RNA) Pyrimidines: Tymine (DNA) / Uracil (RNA)
Guanine (DNA and RNA) Cytosine (DNA and RNA)

DNA – deoxyribonucleic acid


RNA – Ribonucleic acid

DNA: contains all the information


requiredto build the cells and tissues of
an organism (genetic material), 2
strands.
RNA: In the process of transcription, the
information stored in the DNA is copied
into RNA , which has 3 distinct roles in
protein synthesis, 1 strand.
 Messenger RNA: carries the
instruction from DNA that specify
the correct order of amino acids
during protein synthesis, it occurs
during translation of mRNA.
 Transfer RNA: it acts as a
intreperter of an mRNA during
translation.
 Ribosome RNA: “AID” RNA during
tranlation.

DNA structure:
- Primary Stucture: sequence of nucleotides (phosphodiester
bonds).

- Secondary Structure: (double Helix model)


Two polynucleotides chain wound around each other in a
right-handed double helix. The 2 chains are antiparallel(show
opposite polarity),that is why the two strands are oriented in
diferent directions, one on the 5’ to 3’ way and other to 3’ to
5’ way, where 5’ end is the head and 3’ head is the tail.

The bases of opposite strands are


bonded together by hydrogen bonds,
where A with T (two hydrogen
bonds)and G with C (three hydrogen
bonds).

Chargaff’s rule: (A=T) and G=C) , based


on that the sum of the purines equals the
sum of pyrimidines (A+G)=(G+T)

 The base pairs are 3.4 nm apart in DNA Helix.


 A complete 360˚ turns of takes 3.4nm
 There are 10 bases pairs per turn

- Tertiary Structure: DNA supercoiling is


importante for DNA packing whithin all cells.
Supercoiling of DNA reduces the sace and allows for
a loto f more DNA to be package. (superhelix).
RNA structure:
CELL BIOLOGY
Mathias Schleiden (1838) – concluded that all plants are composed of cells.
Theodor Schwann (1839) – concluded that all animals are composed of cells
Rudolph Virchow (1855) – determined that cells come only from other cells.
The cell Theory:
- All organisms are composed of one or more cells.
- Cells are the smallest living thing, the basic units of organization of all organisms.
- Cells arise only by division of a previously existing cell.
The celular level of organization:
Living things are constructed by cells, they can be unicellular or multicellular.
Cell structure is diverse but all cells share common characteristics.
The basic structural and functional unit of every organismo is one of the two types: prokaryotic
or eukaryotic.

2.1. Prokaryotic cells

Include Bacterias and archea.


Bacterial cells have these constant features:

- Cell Wall – Each bacterium is enclosed by a rigid cell wall composed of peptidoglycan =
murein, a protein sugar(polysacharide) molecule. The wall gives the cell its shape and
surronds the..
- cytoplasmatic mebrane, protecting it form the enviroment . It also helps to anchor
appendages like cytoplasm membrane and protrude through the wall to the outside.
The strength of a wall is responsible for keeping the cell from bursting when there are
large diferences in osmotic pressure between the cytoplasm and the enviroment.
- Cytoplasm
- Ribossomes (cytoplasm)
- Innumerable enzymes (cytoplasm)
- Circular Chromossome (DNA) – (Nucleoid)
- Plasmids
- Flagella “most bacterias have” (not present in every prokaryotic cell)
- Fimbriae (pili) (not present in every prokaryotic cell)
Using a techinique – Gram stain, scientist can classify many bacterial species into two gropus
based on cell wall composition:

Gran – positive Gran- negative


Have a cell wall with large amount of Have less peptidoglycan, and it is located in a
peptidoglycan that traps te violet dye in the layer between the plasma menbrane and
cytoplasm. outer membrane.

- Cytoplasmatic mebrane: is a biological membrane that separates the interior of all cells
from the outside environment. The cell membrane is selectively permeable to ions and
organic molecules and controls the movement of substances in and out of cells.

- Cytoplasm:It comprises cytosol(the gel-like substance, composed of water, enzymes,


nutrients, wastes, and gases, also cell structures such as ribosomes, a chromosome and
plasmids), it is where the function for a cell growth, metabolism, and replication is
carried out.

- Ribossomes: They translate the genetic code from molecular language of nucleic acid
to amino acids, so they build blocks of proteins. Bacterial ribosomes are smaller and are
never bound to other organelles, they are free standing structures throughout the
cytoplasm.

- Plasmids: A plasmid is a small, circular, double-stranded DNA molecule that is distinct


from a cell's chromosomal DNA. Plasmids naturally exist in bacterial cells, and they
also occur in some eukaryotes. Often, the genes carried in plasmids provide bacteria
with genetic advantages, such as antibiotic resistance, resistance to heavy metals, and
virulence factors necessary for infection of animal or plant hosts.

- Flagella “most bacterias have” : is a hair-like, that provide a way of locomotion for those
bacterias that have them. They can be found at either both ends of a bacteria or all over
its surface.
- Fimbrae (pill): is short hair-like structures on the surfaces of proKaryotic cells. Like
flagella. Fimbriae are shorter and stiffer than flagella, and slightly smaller in diameter.
2.2 Eukaryotic cells

2.2.1. Plasma /Cell membrane

 Flexible
 Selective permeability (import + export)
 Ingredients: Lipids, Proteins, Carbohydrates -> form fluid mosaic model
 Double layer (bilayer) of lipid molecules (2 parallel sheets of phospholipids)
 Surround organelles
 Separate extracellular fluid from intracellular fluid

Membrane Lipids
 Phospholipids (polar): Glycerophospholipids, Sphingophospholipids
 Sterols (non-polar): Cholesterol
 Structure: Amphipathic
Hydrophilic head (phosphate group)
Hydrophobic tail (2 fatty acids, saturated/unsaturated)

 Membrane fluidity: weak bonds allows mobility:


-Rotation
-flip flop (switching from one phospholipid to another)
- lateral movement (switching position between 2 phospholipids)

 membrane fluidity is influenced by unsaturated hydrocarbon tails (more fluidity than


saturated tails)

Membrane Proteins
 Half of plasma membrane
 Integral proteins
-Inserted into lipid bilayer
-Hydrophobic and hydrophilic regions, allows to interact with inside and outside -
the cell
-Some form channels, pores or carriers -> molecules or ions can move through
 Peripheral proteins
-Not embedded in lipid bilayer
-Many kinds of peripheral proteins: attached to integral proteins, enzymes,
motor proteins, some that link cells together

2.2.2. Nucleus

 Information center and control center for cell


 Contains most of the genes
 Most cells have only on nucleus (e.g. some liver cells are polynuclear)
 All our body cells have a nucleus, except red blood cells (anucleate)
 Without nucleus, cell cannot produce mRNA, proteins

3 Structures of Nucleus:
 Nuclear envelope (membrane):
- Double membrane
- Outer one is continuous with rough ER and ribosomes
- Inner one is lined by nuclear lamina
- Nuclear pores (aqueous transport channel, regulate entry and exit of molecules e.g.
mRNA)
- Selectively permeable
- Nucleoplasm, contains nutrients, salts, semifluid medium inside the nucleus
 Nucleolus/Nucleoli
- Not membrane bounded
- In the nucleus
- Formed around nucleolar organizing regions -> particular part of a chromosome
where nucleolus is formed around
- Manufactur subunits that combine to form ribosomes

 Chromatin
- Chromosomes are made of chromatin
- Composed of DNA, Histone proteins, RNA
- Fundamental unit = nucleosomes

2.2.3.Cytoplasm

- Cellular region between nuclear and plasma membranes


- Consists of cytosol, organelles and inclusion
- Viscous fluid
- Storage substances

2.2.3.1.Cytosol

- Water, proteins, salts, sugars

Cytoskeleton
- Dynamic structure, network of filaments and tubules
- Extend from nucleus to plasma membrane
- Protect cell
- Enables cellular motion
- Role in intracellular transport and cellular division
- Mechanical support
- Composed of: microtubules, microfilaments, intermediate filaments
- These are responsible for: Cell shape, movement of the cell and within the cell
Microtubules:
- Hollow tube
- Constructed from protein tubulin
- Each protein is made up pf 2 subunits
- Shape and support cell
- Guiding movement of organelles
- Separate chromosomes during cell division
- Cilia and Flagella specialized microtubules, involved in cell movement

Microfilaments
- Occur in bundles or mesh like networks
- Actin
- Bear tension, resisting pulling forces

Intermediate filaments:
- Composed of proteins
- NOT involved in cellular movement or contraction
- Reinforce cell shape
- Fixing position of certain organelles
- More permanent

2.2.3.2.Cytoplasmic organelles

Mitochondria
- Convert energy (cell use for work)
- small amount of DNA
- semiautonomous organelles
- double membrane (phospholipid bilayer), surrounded fluid-filled matrix (enzymes)
- outer is smooth and has porins for ions and molecules
- inner are cristae (house protein complexes that produce ATP)
- own genetic material ( double stranded circular DNA)
- cellular respiration
Ribosomes
- made of ribosomal RNAs and protein
- carry out protein synthesis
- two globular subunits
- no membrane
- free ribosomes are in cytosol/cytoplasm
- bound ribosomes attached to ER or nucleus
- can also be found in mitochondria and chloroplast
- make proteins

Endoplasmic reticulum
- system of membranous channels and saccules
- separates internal compartment called ER lumen or cisternal space from cytosol
- rough ER (outer surface has ribosomes), protein synthesis and processing,
membrane factory, distribute transport vesicles
- smooth ER (without ribosomes), function in metabolic processes, synthesis of lipids,
detoxification of drugs and poisons, metabolism of carbohydrates,
- skeletal and cardic muscle cells have smooth ER called sarcoplasmic reticulum play
role in calcium ion storage.

Golgi apparatus
- stack of curved saccules
- receive protein, lipid filled vesicles from ER, packages, processes and distribute
them with cell
- center of manufacturing, warehousing, shipping, sorting
- modify, concentrate, package proteins and lipids from ER
- cis and trans face

Lysosomes
- vesicles produced by golgi apparatus
- contain hydrolytic enzymes
- hydrolyze proteins, fats, polysaccharides, nucleic acids
- recycle cells own organelles and macromolecules

Peroxisomes
- vesicles that contain enzymes
- these use up oxygen and produce hydrogen peroxide and convert it to water
- abundant in liver, produce bile salts, cholesterol, break down fats, detoxify alcohol
- break fatty acids, neutralization of dangerous free radicals
- bounded by single membrane

Plastids
- manufacture
- storage of important chemical compounds
- contain pigments (for photosynthesis)

Cell wall
- made of cellulose
- also present in fungi and yeast, but made of chitin
- freely permeable (plants)
- support and protect plant

Chloroplast
- type pf colored plastids
- varies in shape
- number varies from plant to plant
- bounded by double membrane (chloroplast envelope)
- fluid filled
- contains enzymes
- membranes inside: thylakoids (house chlorophyll -> absorb solar energy,
photosynthesis)
- stroma, granum, thylakoids

Vacuoles
- carry out hydrolysis
- store substances
- no basic shape or size

2.2.4. Plant Cell vs. Animal Cell

Plant and Animal cell ONLY in Plant ONLY in Animal

-Plasma membrane -Cell wall -Centrosome


-Cytoplasm -Chloroplast -Lysosome
-Nucleus -Plastids -Centrioles
-Ribosomes -Cellulose cell walls
-Mitochondria
-Peroxisomes
-Vacuoles (not in every
animal cell and large in plant
cells)
-Flagella (sometimes)
-ER
-Microtubules
-Golgi apparatus
-Chromosomes

2.4. Transport of substances across membrane

Solvent + Solute = Solution


 Hypotonic (low concentration) -> gain water, bloated and burst (in animal cells)
 Hypertonic (high concentration) -> loose water, shrink (in animal cells)
 Isotonic (equal concentration)

2.4.1. Passive (without energy):

 Diffusion
Simple diffusion Passage of small, hydrophobic nonpolar molecules from higher to
lower concentration (e.g. oxygen diffuses from blood into cells, because of higher
concentration)

 Osmosis
Movement of water through membrane, from less concentrated to more concentrated
solution, depends on water
 Aquaporins, water specific channels e.g. in kidneys

 Facilitated Diffusion (with channel/carriers)


Use integral membrane proteins to help move larger, charged, hydrophilic and polar
molecules down the concentration gradient

 Channel Proteins: provide corridors to cross membrane (mostly for ions or water)
 Carrier Proteins: bind molecule for transport through membrane (from high to low
concentration)

2.4.2. Active (with energy)

- Use of bond energy of ATP to move solutes across membrane


- Pumping of the substances across a membrane by a transmembrane protein pump
molecule
- Primary active transport: energy comes directly from hydrolysis of ATP
- Secondary active transport: indirectly from energy stored in ionic gradients
(created by operation of primary active transport pumps)

Active transport
Vesicular transport: transport of large particles (proteins, polysaccharides, nucleic acids)
1) Endocytosis: substances from exterior to interior of cell
2) Exocytosis: substances from interior to exterior of cell

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