BIOCHEMISTRY LEC MIDTERMS to do mechanical, chemical, osmotic,

and electrical work.

Excretion a process by which organisms remove harmful

metabolic wastes from the body. The mode of excretion
is completely different in unicellular and multicellular
organisms.

Transportation, during metabolism, a cell produces

some useful substances (need to be transported to
other cells) and some waste products (need to be
eliminated).

The goal of biochemistry is to explain all life processes in Respiration is a process of the biochemical oxidation of
molecular detail. nutrients at the cellular level.

The foundation of Biochemistry • It occurs in the presence of specific enzymes at

optimum temperatures in the cells to release
- About 15 million years ago, the universe energy for various metabolic activities.
emerges as a cataclysmic eruption of hot, • Equation: Food + oxygen Carbon dioxide
energy-rich subatomic particles.
+ water + energy
- Abou 4 million years ago, life arose – simple
microorganisms existed. Nutrition is the process of an organism acquiring the
food which s needed for its nourishment and for the
DISTINGUISHING FEATURES OF LIVING ORGANISM sustenance.
- Mechanism for sensing and responding to TWO MAIN TYPES OF NUTRITION
alterations in their surroundings.
o Adjusting to changes/ Environmental • Autotrophic
changes • Heterotrophic
- A capacity for precise self-replication and self-
Biomolecules are an organic molecule that includes
assembly
carbohydrates, protein, lipids, and nucleic acids. They
o Bacteria
are important for the survival of living cells.
- A capacity to change over time by gradual
evolution.
o Organisms change their inherited life to
survive in new circumstances.
- Defined functions for each of an organism’s
components and regulated interactions among
them.
o The interplay among the chemical
components of a living organism is
dynamic.
- A high degree of chemical complexity and
microscopic organization.
o Molecules make up a cell’s intricate
internal structures.
- Systems for extracting, transforming, and using
energy from the environment.
o Enabling organisms to build and
maintain their intricate structures and
 Monosaccharides (C6H12O6)

• Carbohydrates isomers
o Glucose
o Galactose
o Fructose

• Monosaccharides are colorless, crystalline solids

that are freely soluble in water but insoluble in
nonpolar solvents.
CARBOHYDRATES
• Most have a sweet taste.
Monosaccharides (simple sugars) – consist of a single • The backbones of common monosaccharides
polyhydroxy aldehyde or ketone unit. are unbranched carbon chains in which all the
carbon atoms are linked by single bonds.
Disaccharides – two monosaccharide units typical is
sucrose (cane sugar), which consists of the six-carbon
sugars L-glucose and L-fructose.

Polysaccharides – are sugar polymers containing more

than 20 monosaccharide units; some have hundreds or
thousands of units.

Example: cellulose and glycogen

Reducing Sugar – a sugar that serves as a reducing

agent due to its free aldehyde or ketone functional
groups in its molecular structure.

SIMPLE CARBOHYDRATES

• Monosaccharides (single sugars)

• Disaccharides (double sugars)

COMPLEX CARBOHYDRATES

• Polysaccharides (many sugars)

Monosaccharides Isomers: each of two or more compounds with the
same formula but a different arrangement of atoms in
• In the open-chain form, one of the carbon
the molecule and different properties.
atoms is doubled-bonded o an oxygen atom to
form a carbonyl group. To represent the three-dimensional structure of sugar,
• Each of the other carbon atoms has a hydroxyl we often use the Fischer projection formulas.
group.
Haworth projections are a simple method to draw cyclic
• If the carbonyl group is at an end of the carbon
sugars while still keeping the stereochemistry of each
chain (that is, in an aldehyde group) the
bond.
monosaccharides an aldose.
• If the carbonyl group is at any other position (in GLUCOSE – dextrose or blood sugar
a ketone group) the monosaccharide is a
• Primary fuel for the body
ketose.
• Found in all disaccharides & polysaccharides.

FRUCTOSE – fruit sugar

• Found in fruit, honey, syrup.

• Converts to glucose in the body.

GALACTOSE – part of lactose

• Found in milk.
• Converts to glucose in the body.

DISACCHARIDES

• Maltose
Simplest monosaccharide has two three-carbon trioses: • Sucrose
• Lactose
• D-Glyceraldehyde, an aldotriose
MALTOSE – malt sugar

• Glucose + Glucose
• Found in germinating seeds & used in
fermentation to produce malted beverages
(beer, whiskey).

CONDENSATION
• Dihydroxyacetone, a ketotriose

Monosaccharides have asymmetric centers

Enantiomers

By convention, designated the D-isomer, the other the L-

isomer. As for the other biomolecules with chiral centers,
the absolute configuration of sugars are known from x-
ray crystallography.
HYDROLYSIS Digestion

• Maltose to Glucose + Glucose • Mouth – salivary amylase

• The disaccharide maltose splits into two glucose • Stomach – fibers and satiety
molecules with H added to one and OH to the • Small intestine – maltase, sucrase, lactase
other (from water). • Pancreas – pancreatic amylase
• Large intestine – fermentation of viscous fibers
SUCROSE – table sugar
o Water, gas, short-chain fatty acid
• Glucose + Fructose production
• Refined from sugar beets & cane

LACTOSE – milk sugar

• Glucose + Galactose
• Lactose intolerance – missing digestive enzyme
needed to split into two monodisaccharide
parts to absorb it.

POLYSACCHARIDES

GLYCOGEN – long chains of glucose found in animals.

• Stored in liver & muscles.

• Helps maintain blood glucose and important
source of “quick energy”, especially during
exercise (lasts only about 12 hours).

STARCH – long chains of glucose found in plants.

• Cereal grains (wheat, rice, corn, etc.), legumes

(beans & peas), and root vegetables (potatoes,
yams).

FIBER

• Component of plant cell walls ABSORPTION

• Classified according to solubility in water.
• Abundant in whole grains, legumes, fruits, and
vegetables
• Examples: cellulose, hemicellulose, and pectin.
Metabolism – a process in which converting food into HEALTH EFFECTS OF SUGAR
energy.
• Sugar in excess
• Glucose in the Body o Contains no nutrients and may
• Used for energy – fuels most of the body’s cells. contribute to malnutrition.
• Stored as glycogen – 1/3 in the liver and 2/3 in o Causes dental caries (tooth decay).
muscles. o Does not cause, but can contribute to:
• Made from protein – gluconeogenesis. obesity, diabetes, heart disease, and
• Converted to fat – when excess of body’s needs. behavioral problems.
• Accusation against sugars
o Sugar causes obesity
Constancy of Blood Glucose o Sugar causes heart disease
• Complex carbohydrates and fiber may reduce
Regulating hormones – maintain glucose homeostasis. the risk of:
• Insulin – moves glucose from the blood into o Heart disease
cells. o Diabetes
• Glucagon – signals the liver to release glucose o GI health
into the blood. o Cancer
o Weight management
• Epinephrine – released when emergency fuel
needed. Soluble Fibers
Diabetes • Lower blood cholesterol by binding dietary
cholesterol so less absorbed.
• Type 1 – failure of insulin production.
• Slow glucose absorption
• Type 2 – obesity
• Slow transit of food through upper GI tract
Hypoglycaemia – rare in healthy people • Holds moisture in stools, softening them.
• Lower risk of heart disease.
Glycaemic response – glycaemic index
• Lower risk of diabetes.
• Gums and mucilages, pectins, psyllium
• Sources:
o Whole-grains, fruits, legumes, seeds
and husks, vegetables.
o Extracted and used as food additives.
• Increase fecal weight – helps form soft, bulky,
stools which improves GI track motility and
reduces risk of constipation, haemorrhoids,
diverticulosis, and colon cancer.
• Speed fecal passage through colon.
• Provide bulk and feelings of fullness (satiety).

Insoluble Fibers

• Cellulose, lignins, hemiculloses

• Sources:
o Brown rice, fruits, legumes, seeds,
vegetables, wheat, bran, whole grains.
o Extracted and used as food additives.
 CHEMICAL PROPERTIES

• Hydrolysis of Triglycerols
o Triglycerides (fats) can be hydrolyzed to
produce glycerol and fatty acids in the
presence of acid and heat or with a
suitable lipase enzyme under biological
conditions.
• Saponification
o Alkaline hydrolysis is termed
saponification because one of the
products of the hydrolysis is a soap,
generally sodium or potassium salts of
fatty acids.
• Hydrogenation
o A process of adding hydrogen atoms to
unsaturated fats until they become
saturated. Hydrogenation of fat is a
process used in industries, food
manufacturers, to synthesize modified
FUNCTIONS OF LIPIDS plant fats called hydrogenated fats that
share similar texture and taste
• Lipids can be used to store energy. characteristics with saturated animal
• Some lipids are important parts of biological fats.
membranes and waterproof coverings. • Halogenation
o Phospholipids o It is a very important property which
• Some circulate in the body as chemical signals determines the degree of unsaturation
to other cells. of the fat or oil that determines its
• Serve as a barrier to exclude water in both biological value.
plants and animals.

CATEGORIES OF LIPIDS
 • Fatty acids are hydrocarbon derivatives.

Saturated Fatty Acids

• A fatty acid with a carbon chain in which all

carbon – carbon bonds are single bonds.

Unsaturated Fatty Acids

• Monounsaturated Fatty Acids (MUFAs)

o Have one double bond in the fatty acid
chain with all of the remainder carbon
atoms being single-bonded.
• Polyunsaturated Fatty Acids (PUFAs)
o Have more than one double bond in the
fatty acid chain.
 LIPIDS AS COFACTORS AND PIGMENTS

LIPIDS AS SIGNALS

STEROID HORMONES ANY MESSAGES BETWEEN

TISSUE

• Testosterone and Estrogen

o Steroid hormones, derived from sterols,
serve as powerful biological signals, such
as the sex hormones.

PROTEINS

• Most structurally & functionally diverse group of

biomolecules.
• Functions:
o Involved in almost everything.
▪ Metabolism
▪ Support
▪ Transport
▪ Regulation
▪ Motion
Metabolism • Receptor Proteins
o Build into the membranes of nerve cells.
• Enzymes
o Detect chemical signals
o Biological catalyst – speed up chemical
(neurotransmitters) released by other
reactions.
nerve cells.
o Digestive enzymes aid in hydrolysis.
▪ Lipase – uses to break down fats Motion
in food.
• Muscle contraction
▪ Amylase – digest starch into
o Actin and myosin – make up muscle
smaller molecules.
fibers.
▪ Lactase – helps to digest lactose.
▪ Protease – regulate the fate, • Motor proteins within the cell.
localization, and activity of many o Allow cell components to move from
proteins. place to place.
o Molecular Biology o Flagella – move the cell.
▪ Polymerase – responsible for o Cilia – move contents around the cell.
forming new copies of DNA.
▪ Ligase – links two fragments of
DNA by forming a PROTEIN STRUCTURE & FUNCTION
phosphodiester bond. Function depends on structure.
Support • 3-D structure
• Structural proteins o Twisted, folded, coiled into unique
o Keratin – hair and nails shape.
o Collagen – supports ligaments, tendons, Primary (1°) structure
and skin.
o Silk – cocoons and spider webs. • Order of amino acids in chain.
o amino acids sequence determined by
Transport gene (DNA).
• Channel and carrier proteins in the cell o Slight change in amino acid sequence
membrane. can affect protein’s structure and its
o Allows substances to enter and exit the function.
cell. ▪ Even just one amino acid change
• Transport molecules in blood. can make all the difference.
o Hemoglobin (globulin) – transport Secondary (2°) structure
oxygen in the blood.
• “Local folding”
Defense o Folding along short sections of
• Antibodies polypeptide.
o Combat bacteria and viruses ▪ Interaction between adjacent
amino acids.
Regulation ▪ H bonds between backbones
(O:H)
• Hormones
▪ α-helix
o Intercellular messengers that influence
▪ ß-pleated sheet
metabolism
▪ Fibrous proteins – only have
o Insulin – regulates the amount of glucose
secondary structure.
in the blood and in cells.
• Keratin
o Human growth hormone – maintaining
normal body structure and metabolism. • Silk
Tertiary (3°) structure NONPOLAR AMINO ACIDS

• “Whole molecule folding”. • Nonpolar & hydrophobic

o Created when the secondary structure
fold and form bonds to stabilize the
structure into a unique shape.
o Determined by interactions between R
groups.
▪ Hydrophobic interactions
▪ Anchored by disulfide bridges
▪ Ionic bonds between R group
▪ Hydrogen bonds between
backbones.
▪ Van der Waais Force (Velcro)
• Globular (spherical)
POLAR AMINO ACIDS
proteins – have tertiary
structure. • Polar or charged & hydrophobic.
• Enzymes

Quaternary (4°) structure

• Two or more tertiary folded peptide subunits

bonded together to make a functional protein.
o Hemoglobin – 4 polypeptides
o Collagen – 3 polypeptides

Denature a protein

• Unfolding a protein/changes the shape.

o Disrupt 3° structure
▪ pH
▪ temperature
o unravels or denatures protein
o disrupts H bonds, ionic bonds & disulfide
bridges.
o Destroys functionality PROTEINS

• Structure;
AMINO ACIDS o Monomer = amino acids
▪ 20 different amino acids
• Structure • 12 made by body.
o Central carbon (α carbon) • 8 essential amino acids
o Amino group (must get from food)
o Carboxyl group (acid) o Polymer = polypeptide
o R group (side chain) ▪ Protein can be one or more
▪ Variable group polypeptide chains folded &
▪ Confers unique chemical bonded together.
properties of the amino acid. ▪ Large & complex molecules
▪ Complex 3-D shape.
ESSENTIAL, NONESSENTIAL, AND CONDITIONAL

• Essential – must be consumed in the diet.

• Nonessential – can be synthesized in the body.
• Conditionally essential – cannot be synthesized
due to illness or lack of necessary precursors.
o Premature infants lack sufficient
enzymes needed to create arginine.

Condensation and hydrolytic reactions

• A peptide bond forms by condensation when the

acid group (COOH) and amine group of two
different amino acids join and release a molecule
of water.
• When peptide bonds are broken by hydrolysis,
the hydroxyl group (OH) and hydrogen (H) from
water are added.

Building proteins

• Peptide bonds
o Linking NH2 of one amino acid to COOH
of another.
o C-N bond
o N terminus – C terminus