PROTEINS

c.) Tertiary Structure

-long chains of amino acids that form the
basis of all life
-large, complex molecules that play many
critical roles in the body
-there are 20 different amino acid that can
be combined to form protein
-the protein molecule will bend and
twist in such a way as to achieve
maximum stability or lowest
energy state.

4 PROTEIN STRUCTURES

a.) Primary structure

-unique order of amino acids that
linked together to form a protein
-all amino acids have the alpha carbon
bonded to a hydrogen atom,
carboxyl
group, and an amino group.
d.) Quaternary structure
-structure of a protein macromolecule
formed by interactions between
Multiple polypeptide chains “subunits”

b.) Secondary structure

-coiling or folding of a polypeptide chain
that gives the protein its 3-D shape
-(α)helix -coiled spring and secured by
BASIC STRUCTURE OF AMINO ACID
hydrogen bonding in the polypeptide
chain
-(β)pleated sheet -folded or pleated and
is held together by hydrogen bonding
between polypeptide units of the folded
chain

-all amino acids are ampholytes, each

contains an amino and carboxyl group
-H and -COOH groups bound to the
alpha C are both ACIDIC
-the basic characteristic of the amino
acid is due to the lone pair of electrons
of the amino group
-naturally occurring amino acids belong Tyrosine Asparagine
the a-configuration

*ampholytes - compounds that when

dissolved in water can act either as acid
or as a base

Glutamine
DIFFERENT CLASSES OF AMINO
ACIDS

Alanine Cysteine

NON-POLAR AMINO ACID

Alanine Valine

Aspartic Histidine

Leucine Phenylalanine

Isoleucine Tryptophan

POLAR AMINO ACIDS

Serine Threonine

Proline Cysteine
 Methionine Glycine
MIRROR IMAGE OF AMINO ACID

ACETIC AMINO ACID

Aspartic Glutamic

-the a-COO group is directed up and behind

the plane of the page, and the R-group is
directed down and behind the plane of the
page. The a-h and a-NH3+ groups are
directed toward the reader
BASIC AMINO ACID -if the a-NH3+ is projected to the left the
amino acid has an L absolute configuration
Histidine Lycine -its optical enantiome, with a-NH3+
projected toward the right, has a D
absolute configuration

PEPTIDE BOND FORMATION

Arginine
-this polymerization is a dehydration
reaction

-the a-carboxyl group of an amino acid with

side chain R1 forms a covalent peptide bond
with the a-amino group of the amino acid
with side chain R2 by elimination of a
molecule of water
Neutral side chains:
-the amino acid is neutral unless there is an
-the dipeptide can form a second peptide
extra acid or base on the side chain. If
bond through its terminal carboxylic acid
neither is present then the whole amino
group and the a-amino of a third amino
acid is neutral
acid (R3), yo generate a tripeptide