BIOMOLECULES DEHYDRATION SYNTHESIS

1. Hydrogen atom is removed from one

ORGANIC MOLECULES monomer
● molecules that contain carbon and 2. A hydroxyl group (OH) is removed
other elements held together by from monomer it is to be joined with
covalent bonds 3. A covalent bond then forms, uniting
● the name organic came about at a the monomers
time when scientists believed that all 4. A water molecule is released
organic molecules were created only ● This removal of a water molecule
by living organisms and all inorganic (dehydration) at the bond site occurs
molecules came from nonliving each time a monomer is added to
matter the growing polymer chain
● The synthesis of larger molecules by
CARBON dehydration synthesis requires
● relatively rare in the natural world, energy (condensation reaction)
representing less than 0.03% of
Earth’s crust HYDROLYSIS
● accounts for about 18% of body 1. A water molecule is added to bond
weight in humans 2. The bond is broken
● common building block of all organic 3. Monomers are released
molecules because of the many ● The equivalent of a water molecule
ways it can form strong covalent is added each time a covalent bond
bonds with other atoms between single subunits in the chain
● has six electrons; two in the first is broken
shell and four in the second ● Reverse of dehydration synthesis
● most stable when its second shell is ● Used to break down molecules of
filled with eight electrons = forms food during digestion, to recycle
four covalent bonds with other materials for reuse, and to get rid of
molecules substances that are no longer
needed by the body
ORGANIC COMPOUNDS
● most organic compounds are very
large molecules
● interactions with other molecules
involve only functional groups
● many organic compounds are
polymers
● Polymers = are chainlike molecules
made of many similar or repeating
units (monomers), which are joined
together by dehydration synthesis
CARBOHYDRATES
● contain carbon, hydrogen, and
oxygen (CH2O)
● hydrogen and oxygen atoms appear
in the same ratio as in water; two
hydrogen atoms to one oxygen atom
● Carbohydrate = “hydrated carbon” 2. Disaccharides
● classified according to size and ● known as “double sugars”
solubility in water ● formed when two simple
TYPES OF CARBOHYDRATES sugars are joined by
1. Monosaccharides dehydration synthesis (water
● one = (mono); sugar = molecule is lost as the bond
(saccharide) forms)
● known as the simplest kind of ● double sugars are too large
carbohydrate or simple to pass through
sugars ● must be broken down
● have single-chain or single- (digested) to their
ring structures (carbon monosaccharide units to be
backbone forms either a line absorbed from the digestive
or a circle) tract into the blood through
● most common contain five or hydrolysis
six carbon atoms arranged in ❖ Sucrose = glucose-fructose; cane
five- or six-membered ring sugar
● Glycosidic Linkage = joins ❖ Lactose = glucose-galactose; in milk
a carbohydrate molecule to ❖ Maltose = glucose-glucose; malt
another group, which may or sugar
may not be another
carbohydrate
● Aldoses = carbonyl group at
end of carbon skeleton
● Ketoses = carbonyl group
within carbon skeleton
● Linear Form = long
3. Oligosaccharides
● Ring Form = most stable
● oligo = few
form
● short strings of
❖ Glucose = called blood sugar;
monosaccharides linked
universal cellular fuel
together by dehydration
❖ Fructose & galactose =
synthesis
converted to glucose for use by
● covalently bonded to certain
body cells
cell-membrane proteins
❖ Ribose & deoxyribose = form
(glycoproteins)
part of the structure of nucleic
● Glycoproteins = participate
acids and genetics
in linking adjacent cells
 together and in cell-cell ● building blocks of proteins are small
communication molecules called amino acids
● each amino acid has an amino
4. Polysaccharides group NH3 (gives basic properties)
● long, branching chains of on one end, a carboxyl group on
linked simple sugars the other, a COOH group (allows to
● known as “many sugars” act as acid) in the middle
● large, insoluble molecules ● all amino acids are identical except
= ideal storage products for a single group R-group
● lack the sweetness of simple ● differences in the R-groups make
and double sugars each amino acid chemically unique
❖ Starch = storage polysaccharide ● differences in the charge and
formed by plants; grain products and structure of the amino acids affect
root vegetables the shape and functions of the
❖ Glycogen = slightly smaller, but proteins constructed from them
similar, found in animal tissues ● our bodies can synthesize (make)
11 of the amino acids if necessary
❖ Polypeptide = single string of 3 to
100 amino acids
= a protein longer than 100 amino
acids and has a complex structure
UTILIZATION OF GLUCOSE and function
1. Glucose is oxidized or “burned” by
STRUCTURAL LEVELS OF PROTEINS
combining with oxygen) in a complex
1. Primary Structure
set of chemical reactions
● sequence of amino acids
2. It is broken down into carbon dioxide
composing each amino acid
and water
chain
3. Some of the energy released as the
● backbone of a protein
glucose bonds are broken is trapped
molecule in which the
in the bonds of high-energy ATP
chemical properties of each
molecules, the energy “currency” of
amino acid will affect how the
all body cells
protein folds
4. If not needed for ATP synthesis,
dietary carbohydrates are converted
to glycogen or fat and stored

PROTEINS
● account for over 50 percent of the
organic matter in the body 2. Secondary Structure
● have the most varied functions of all ● how the chain of amino acids
organic molecules is oriented in space
● contain carbon, oxygen, hydrogen, ● proteins can coil into an
nitrogen and sulfur almost infinite variety of
 seemingly random shapes of hydrogen bonds that hold
depending on which amino the whole sequence
acids make up the sequence ● covalent bond disulfide
❖ Types of Secondary: (S¬S) bond forms between
A. Alpha (a)- helix the sulfur molecules of two
● right-hand spiral formed by cysteine amino acids
coiling of the primary chai ● acquire this structure by a
● stabilized by hydrogen bonds folding process that occurs
● h-bonds always link different either during synthesis or
parts of the same chain shortly thereafter
B. Beta (b)-pleated sheet
● do not coil
● linked side by side by
hydrogen bonds
● form a pleated, ribbonlike
structure
● h-bonds may link together
different polypeptide chains
as well as different parts of
4. Quaternary Structure
the same chain
● how many polypeptide
chains make up the protein
(if there is more than one)
and how they associate with
each other

3. Tertiary Structure
● how the protein twists and
folds to form a three-
dimensional shape
● depends on its sequence
of amino acids
● locations of the polar and
charged groups within the
chain determine the locations
 ● water-soluble proteins that play
crucial roles in biological processes
PROTEIN STRUCTURES
● links that determine the secondary
and tertiary structures of protein are
relatively weak hydrogen bonds
● they may be broken by nearby
charged molecules
● shape of proteins can change in
the presence of charged or polar
molecules
● can also be damaged, sometimes
permanently, by high temperatures
or changes in pH A. Antibodies (immunoglobulins)
● Denaturation = permanent ● recognize, bind with, and
disruption of protein structure, inactivate bacteria, toxins, and
leading to a loss of biological some viruses
function ● function in the immune
response, which helps protect
❖ Fibrous/Structural Proteins the body from “invading”
● appear most often in body structures foreign substances
● exhibit only secondary structure, B. Hormones
● but most have tertiary or even ● help to regulate growth and
quaternary structure development
● important in binding structures ● Growth hormone = optimal
● provide strength in body tissues growth
● collagen in bones, cartilage, and ● Insulin = blood sugar levels
tendons and keratin in hair and nails ● Nerve growth factor =
and skin growth of neurons
C. Transport proteins
● Hemoglobin transports
oxygen in the blood
● other transport proteins in the
blood carry iron, cholesterol,
or other substances
D. Enzymes (catalysts)
● Catalyst = substance that
speeds up the rate of a
chemical reaction without
being altered or consumed
❖ Globular/Functional Proteins
by the reaction
● mobile, generally compact, spherical
● increase the rates of
that have tertiary structure
chemical reactions
 ● help biochemical reactions to
occur, but they do not
change the final result of the
reaction
● can only speed reactions that
would have happened
anyway, although much more
slowly
● in their absence, biochemical
reactions cease
● serve as catalysts because E. Defensive Proteins – protect
as proteins they can change against disease
shape F. Storage Proteins – store amino
ENZYME ACTIVITY acids
● Substrate = molecule acted upon by G. Receptor – receive signals from
an enzyme outside cells
● Active Sites = “fit” and interact H. Motor Proteins – function in cell
chemically with substrates movement
= allows weak bonds to be formed I. Structural Proteins – provide
between the two molecules structural support
● Enzyme-substrate complex
= structure formed when substrates 20 AMINO ACIDS
are bound to the active site
1. Two reactants, each with a shape ● Nonpolar (hydrophobic)
that corresponds to a specific 1) Glycine 2) Leucine 3) Phenylalanine
binding site on the enzyme, 4) Alanine 5) Isoleucine 6) Tryptophan
approach the enzyme 7) Valine 8) Methionine 9) Proline
2. The reactants bind to the enzyme
at their respective binding sites. ● Polar (hydrophilic)
3. The binding of both substrates to the 10) Serine 11) Cysteine 12) Asparagine
enzyme triggers a change in the 13) Threonine 14) Tyrosine 15) Glutamine
enzyme’s shape
4. The reactants are brought together, ● Electrically charged side chains
and a dehydration synthesis (hydrophilic)
reaction occurs 16) Aspartic Acid 17) Lysine 18) Histidine
5. The binding of the two substrates 19) Glutamic Acid 20) Arginine
together triggers another change in
the enzyme’s shape, and the final Cysteine = the only amino acid with sulfur
product is released
6. Note that the enzyme is not used
up during the reaction; once the
product is released the enzyme is
able to repeat the process again
with new substrates LIPIDS
 ● enter the body in the form of meats, = tails are fairly straight,
egg yolks, dairy products, and oils allowing them to pack closely
● contain carbon, hydrogen, and together
oxygen atoms, but in lipids, carbon = solid at room temperature
and hydrogen atoms far outnumber = Ex: animal fats, such as
oxygen atoms butter and bacon grease
● illustrated by the formula for a typical = diet rich in saturated fats is
fat named tristearin, which is thought to contribute to the
C57H110O6 development of
● insoluble in water but readily cardiovascular disease
dissolve in other lipids and in organic
solvents such as alcohol and ❖
acetone
● stored in adipose (fat) tissue and are
an important source of stored energy
in our bodies

TYPES OF LIPIDS
1. Triglycerides
● composed of two types of Unsaturated fats (oils) = fewer than
building blocks, fatty acids two hydrogen atoms on one or more
and glycerol of the carbon atoms in the tails
● synthesis involves the = double bonds form between
attachment of three fatty adjacent carbons, putting
acids to a single glycerol kinks in the tails and
molecule preventing the fats from
● result is an E-shaped associating closely together
molecule that resembles the = liquid at room temperature
tines of a fork
● Fatty acids = chains of ❖
hydrocarbons (usually about
16 to 18 carbons long) that
end in a group of atoms
known as a carboxyl group
(HO¬C==O)
● Fats vary in the length of
their fatty acid tails and the
ratio of hydrogen atoms to
carbon atoms in the tails Trans fats = common in many
❖ Saturated fats = have a full margarines and baked products
complement of two hydrogen atoms = are oils that have been
for each carbon in their tails solidified by the addition of
hydrogen atoms at sites of
double carbon bonds, which
 reduces those bonds to single neutral and relatively
carbon bonds insoluble in water
= increase the risk of heart
disease by raising “bad” 3. Steroids
cholesterol and decreasing ● do not look at all like the
“good” cholesterol lipids described previously
❖ Omega-3 fatty acids = found ● classified as lipids because
naturally in cold-water they are relatively insoluble
= appear to decrease the risk in water
of heart disease and some ● consist of a backbone of
inflammatory diseases. three 6-membered carbon
rings and one 5-membered
carbon ring to which any
number of different groups
may be attached
❖ Cholesterol = earned bad press
because of its role in arteriosclerosis
= found in cell membranes
and is raw material used to
make vitamin D, steroid
hormones and bile salts
= vital to homeostasis
2. Phospholipids =structural component of
● modified form of lipid animal cell membranes
● primary structural component =source of several important
of cell membranes hormones, including the sex
● have a molecule of glycerol hormones estrogen and
as the backbone, but they testosterone
have only two fatty acid tails.
● replacing the third fatty acid
is a negatively charged
phosphate group (PO4-)
● another group that varies
depending on the
phospholipid but is positively
charged
● presence of charged groups
on one end gives the
phospholipid a special
property: One end of the
molecule is polar and thus
soluble (dissolves) in water
● the other end (represented
by the two fatty acid tails) is