Proteins determined by the chemical interactions between

amino acids.
8.1:Intro to Protein
3. Tertiary structure – This is the unique three-
Protein makes up approximately 20 percent of the
dimensional shape of a protein, formed as the different
human body and is present in every single cell. The
side chains of amino acids chemically interact, either
word protein is a Greek word, meaning “of utmost
repelling or attracting each other. Thus, the sequence of
importance.” Proteins are called the workhorses of life
amino acids in a protein directs the protein to fold into
as they provide the body with structure and perform a
a specific, organized shape.
vast array of functions. You can stand, walk, run, skate,
swim, and more because of your protein-rich muscles. 4. Quaternary structure – In some proteins, multiple
folded polypeptides called subunits combine to make
Protein is necessary for proper immune system
one larger functional protein. This is called quaternary
function, digestion, hair and nail growth, and is involved
protein structure. The protein hemoglobin is an
in numerous other body functions. It is estimated that
example of a protein that has quaternary structure. It is
more than one hundred thousand different proteins
composed of four polypeptides that bond together to
exist within the human body.
form a functional oxygen carrier
8.2: Protein Structure
An important concept with proteins is that SHAPE
What Is Protein? determines FUNCTION. A change in the amino acid
sequence will cause a change in protein shape. Each
 Proteins are macromolecules composed of protein in the human body differs in its amino acid
amino acids. For this reason, amino acids are sequence and consequently, its shape. The synthesized
commonly called the building blocks of protein. protein is structured to perform a particular function in
There are 20 different amino acids, and we require all of a cell. A protein made with an incorrectly placed amino
them to make the many different proteins found acid may not function properly, and this can sometimes
throughout the body. Proteins are crucial for the cause disease. An example of this is sickle cell anemia, a
nourishment, renewal, and continuance of life.Just like genetic disorder. When packed in red blood cells to
carbohydrates and fats, proteins contain the elements deliver oxygen, this structure gives red blood cells a
carbon, hydrogen, and oxygen, but donut shape.
In people with sickle cell anemia, DNA gives cells the
 Proteins are the only macronutrient that also incorrect message when bonding amino acids together
contain nitrogen as part of their core structure. to make hemoglobin. The result is crescent-shaped red
In each amino acid, the elements are arranged blood cells that are sticky and do not transport oxygen
into a specific conformation, consisting of a like normal red blood cells, as illustrated in the figure
central carbon bound to the following four below.
components:
 A hydrogen The specific three-dimensional structure of proteins can
 A nitrogen-containing amino group be disrupted by changes in their physical environment,
 A carboxylic acid group (hence the name causing them to unfold. This is called denaturation, and
“amino acid”) it results in loss of both structure and function of
 A side chain proteins. Changes in pH (acidic or basic conditions) and
exposure to heavy metals, alcohol, and heat can all
The first three of those components are the same for all cause protein denaturation.
amino acids. The side chain—represented by an “R” in
the diagram below —is what makes each amino acid The proteins in cooked foods are at least partially
unique. denatured from the heat of cooking, and denaturation
in the stomach is an important part of protein digestion,

We can see everyday examples of denaturation in

cooking techniques, like how egg whites become solid
and opaque with cooking, and cream becomes fluffy
when it’s whipped.

Both are examples of denaturation leading to physical

changes in protein structure, and because protein
Protein Organization structure determines function, denaturation also causes
proteins to lose their function.
Protein’s structure enables it to perform a variety of
functions. There are four different structural levels of
proteins (Figure 6.6.):

1. Primary structure – This is the one-dimensional

polypeptide chain of amino acids, held together by
peptide bonds.

2. Secondary structure – The polypeptide chain folds

into simple coils (also called helices) and sheets,