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the order (sequence) of amino acids in a protein, which is specified by the order
(sequence) of nucleotides in a gene, is called its primary structure.
Primary (1o)
Secondary (2o)
Tertiary (3o)
Quaternary (4o)
Today we will examine the monomeric constituents of proteins (the amino acids)
an important concept is that with respect to the fully folded and active protein,
everything depends upon the primary sequence of the amino acids in
the protein
Later we will examine the 1o, 2o, 3o, 4o structure of proteins.
H2N C C
OH
H
Note that the structure of amino acids can be depicted in various ways
HO
H2N C C
OH
H
is the
same as
H2N C H
R
or
H2N C C
R
OH
The amino and carboxyl group can be ionized depending on the surrounding pH.
At the pH typical of cytoplasm (pH 6.8 7.4, physiological pH) the amino group will be
protonated and the carboxyl group will be deprotonated.
Thus we typically draw amino acids in this form:
H3N C C
O
H
The
zwitterionic form of
an amino acid
The side chain (or R group) for each amino acid is unique
Imparts unique chemical character to each amino acid
Amino acids are therefore largely defined by the side chain
Major side chain characteristics:
Apolar (or non-polar or hydrophobic)
Polar and (or hydrophilic) (but uncharged)
Negatively charged (Acidic) - full ionic negative charge
Positively charged (Basic) - full ionic positive charge
H3N C C
O
H
Hydrophobic
Hydropathy Scale
-the relative hydrophobicity
of amino acids
Hydrophilic
Recall
Hydrophobic Interactions
Hydrophobic interactions occur between molecules that cannot interact with water.
Consider mixing oil and water. Oil molecules are called APOLAR because they
cannot interact with water (through Hydrogen bonding).
They therefore coalesce together (interacting with each other through
Van der Waals forces) and in doing so minimize their surface area contact
with water molecules.
or
hydrophobic
(slides 12-16)
Hydrogen Bonds
A functional group can become a Hydrogen bond donor whenever an H atom is
covalently bonded to an atom that is very electronegative (such as N or O)
because the H atom takes on a partial + charge, as shown below:
donor
acceptor
Water can also dissolve other molecules that are not ionic so long as they are also polar
(e.g. like sugar molecules)
by forming Hydrogen bonds with the molecules.
sucrose
glucose and fructose disaccharide
Hydrophobic molecules (such as oils) cannot dissolve in water because oils are
neither ionic or polar and water molecules therefore cannot electrostatically
interact with them.
Both serine and threonine are polar because they have polar OH groups
One of these is more polar/hydrophilic than the other. Which one is the most polar
amino acid and why?
carboxylate group
carboxyamide group
these are the amino acids with important roles in the active site
some play a direct role in catalysis and these are called CATALYTIC amino acids
others play an accessory role (eg. substrate/TS binding, other interactions) and
are just called active site amino acids