BIOMACROMOLECULES
BIOMACROMOLECULES
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.
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
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.
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.
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
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:
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.
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.
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.
MONOSACCHARIDES
Monosaccharides generally have formulas
that are some multiple of the unit CH2O.
Glucose is the most common
monosaccharide.
COMMON MONOSACCHARIDES
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
COMMON DISSACHARIDES
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.
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
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.
GLYCOSAMINOGLYCANS
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.
1.3.2. Phospholipids
1.3.3. Steroids
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.
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)
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 .
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 structure:
- Primary Stucture: sequence of nucleotides (phosphodiester
bonds).
- 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:
- 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.
- 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.
- 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
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 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
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
2.2.3.1.Cytosol
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
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
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)
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