Biochemistry

Amino acids
Basic

units of proteins (monomers)

Contain both carboxylic (-COOH) and
amino groups (-NH2)

Amino acids
They

can be ,, amino acids,

according to where the amino group
bonds
If the amino group is attached to the
carbon next to the carboxylic carbon,
the amino acid is an a-amino acid. If it is
attached to carbon next to the a-carbon,
the amino acid is a -amino acid, and so
on.

Amino acids
Amphoteric

= they act both as acids

and bases
In basic environment, they have a basic
structure
In acidic environment they have an
acidic structure
At isoelectric point, they have the
amphoteric structure (zwitterion)

Amino acids
Hydrophobic

amino acids

Nonpolar amino acids with aliphatic R

groups:

Amino acids
Nonpolar

groups

amino acids with aromatic R

Amino acids
Hydrophilic

amino acids:

Polar amino acids:

Amino acids
Acidic

amino acids

Amino acids
Basic

amino acids

Amino acids

Peptides.Proteins
More

amino acids form a peptide

More peptides form a protein
An amido linkage formed between two
amino acids is called peptide bond.

Peptides.Proteins
Peptides

can be: dipeptides, tripeptides,

polypeptides
Some hormones have a peptidic
structure: Insulin, Antidiuretic hormone,
calcitonin, ACTH, etc.
When the number of amino acids is over
20-30, and the structure of the
compound is more complex, than we
consider it a protein

Proteins
Primary

structure= sequence of
amino acids in the protein
They have an N-terminal end
(containing NH2 group) and a Cterminal end (containing COOH group)
We usually write proteins (and peptides!
) from the N-terminal to the C-terminal
ends!

Proteins

Secondary structure:

-helix : helical structure in which the long

polypeptide chain is wound around the
long axis. The side chains (R groups) of the
amino acids extend out of the helical
backbone. This conformation of peptide
chain has interactions within its chains by
hydrogen bonding (4 amino acids in one
turn). It is usually found in globin-like
proteins (ex: Hemoglobin)

-pleated sheet: sheet-like arrangement

of the polypeptide chains. The hydrogen
bonds we found between the adjacent
polypeptide chains. The polypeptide
chains involved in the pleated sheet
structure can be either parallel or
antiparallel. Hydrogen bonds stabilize the
P-pleated sheet. It is usually found in
fiber-like proteins, like collagen.

 Tertiary

structure: three dimensional

arrangement of the polypeptide chain.
Different kinds of bonds or interactions
are responsible for the maintenance of
the tertiary structure. They include
hydrophobic forces, hydrogen bonds,
disulfide bonds, salt bridges, and Van
der Waal forces

 Quaternary

structure

For complex proteins, with multiple

subunits
The way in which three-dimensional
subunits interact to form the complete
functional protein
Ex: Hemoglobin

Denaturation of proteins
Protein

denaturation includes the complete

or partial unfolding of the polypeptide chain,
cleavage of disulfide linkages, and breakage
of noncovalent interactions. Denaturation is
sometimes reversible. The reversing process
is called renaturation.
Denaturating factors: temperature, pH,
pressure
Ex: boiling an egg

Proteins
Holopoteins

(only amino acids)

Heteroproteins:

Amino acids
Prosthetic group (metals, sugars, lipids,
phosphoric acid, etc)
Ex: Hemoglobin has Fe3+ as a prosthetic
group

Carbohydrates
Cn(H2O)n
Monosaccharides
Disaccharides
Polysaccharides
Many

OH groups and a carbonyl group

According to the carbonyl group they
are aldose sugars or ketone sugars.

Carbohydrates
Monosaccharides:

3,4,5,6, etc Carbons in the molecule (triose,

tetrose, pentose, hexose, etc)
They have asymmetric carbons, which are
optically active, so they form a lot of
stereoisomers! (2 mirroring isomers are called
enantiomers, 2 stereoisomers which are not
enantiomers are called diastereoisomers and
2 isomers which differ only by one asymmetric
carbon are called epimers)
They can be D-forms or L-forms, according to
which side is the farthest OH group, away from
the carbonyl group

 In

solution they form a cyclic form:

In aldohexoses (like Glucose), the cyclic structure is formed

when the hydroxyl group in the fifth carbon reacts with the
carbonyl carbon of the aldehyde group.
The six-membered (hemiacetal) ring formed is called the
pyranose ring.If the cycle has 5 members (usually for
ketohexoses like Fructose), than it is called a furanose ring.
The resulting OH group can be on either side of the cycle, so
the resulting cyclic structure can either be an a-(same side
of the cycle) or a -anomer (opposite side of the cycle).
In aqueous solutions, the a- and -anomers can
interconvert, and the process is termed mutarotation

 The

saccharides that have an aldolic

group can be oxidized by the Tollens,
Fehling and Benedict solutions!

Disaccharides
Disaccharides are sugar units containing
two monosaccharides linked by a covalent
bond called glycosidic bond.
Ex:
Maltose (two glucoses)
Sucrose (glucose and fructose)
Lactose (glucose and galactose)
The hydrolysis of disaccharides gives their
corresponding monosaccharide subunits.

Polysaccharides
Polymers of monosaccharides
Ex:

Starch
Formed

from amylose (1-4 linked glucoses, soluble in water)

and amylopectin (1-4 and 1-6 linked glucoses, insoluble in
water) polymers.
found in plants!

Glycogen
similar

to the amylopectin (insoluble in water)

Found in animals (stored in muscles and liver, energy source)

Cellulose
-glucoses-people

cannot digest them!

Lipids
Hydrophobic

compounds
Used as energy source, part of cell
membranes, functional lipids (such as
hormones)
Two kinds:

TAG (triacylglycerols)
Steroids

TAG
Formed

by esterification of glycerol and

fatty acids and are used mainly as
storage of energy

Steroids
Used

as functional lipids, especially

hormones (corticosteroids, sex
hormones), but also as structural lipids
(part of cell membrane)
The starting compound is cholesterol,
from where all the others are
synthesized in the human body
Extremely important for the human
body!