3.

7: PROTEINS
polar, (3) acidic, with a net negative charge, and (4) basic, with a net
 PROTEIN SHAKE positive charge at neutral pH.
Proteins can differ from one another in the number and sequence (order)
Drinks like this shake contain a lot of protein. Such drinks are
of amino acids. It is because of the side chains of the amino acids that
popular with people who want to build muscle because muscle tissue
proteins with different amino acid sequences have different shapes and
consists mainly of protein. Making up muscles is just one of a
different chemical properties. Small proteins can contain just a few
plethora of functions of this amazingly diverse class of biochemicals.
hundred amino acids. Yeast proteins average 466 amino acids. The largest
known proteins are the titins, found in muscle, which are composed of
over 27,000 amino acids.

PROTEIN STRUCTURE
Amino acids join together to form a molecule called a dipeptide. The –
OH from the carboxyl group of one amino acid combines with a hydrogen
atom from the amino group of the other amino acid to produce water. This
is called a condensation reaction - a reaction in which two molecules
combine to form a single molecule with a release of water. Figure 3.7.3)
shows this process. The top part of the image shows two amino acids;
note the -OH in amino acid 1 and the -H in amino acid two are
highlighted. These are the atoms that will be removed from the amino
Figure 3.7.1 : Protein shake acids to form water. This allows a covalent bond forms between the
carboxyl carbon of one amino acid and the amine nitrogen of the second
WHAT ARE PROTEINS? amino acid. This reaction forms a molecule called a dipeptide and the
carbon-nitrogen covalent bond is called a peptide bond. When repeated
numerous times, a lengthy molecule called a polypeptide is eventually
produced. Very lengthy polypeptides with functional configuration are
called proteins.
Amino acid (1) Amino acid (2)

N-terminus C-terminus

Peptide bond
Figure 3.7.2 : General Structure of Amino Acids. This model shows the
general structure of all amino acids. Only the side chain, R, varies from
one amino acid to another. For example, in the amino acid glycine, the
side chain is simply hydrogen (H). In glutamic acid, in contrast, the side
chain is CH CH COOH CH2CH2COOH. Variable side chains give
2 2

amino acids different chemical properties. The order of amino acids, Water
together with the properties of the amino acids, determines the shape of
the protein, and the shape of the protein determines the function of the Dipeptide
protein. KEY: H = hydrogen, N = nitrogen, C = carbon, O = oxygen, R = Figure 3.7.3 : Amino acids join together to form a molecule called a
variable side chain. dipeptide. The C−N bond is called a peptide bond. The order of amino
Proteins are organic compounds that contain carbon, hydrogen, oxygen, acids is by convention shown with the free amino group on the left and
the free carboxyl group on the right.
nitrogen, and, in some cases, sulfur. These compounds have many
essential functions within the cell (see below). Proteins are made of Proteins may have up to four levels of structure, from primary to
smaller units called amino acids. There are 20 different common amino quaternary, as described and shown in the diagram below, giving them the
acids needed to make proteins. All amino acids have the same basic potential for tremendous diversity:
structure, which is shown in Figure 3.7.3. Only the side chain (labeled R A protein’s primary structure is the sequence of amino acids in its
in the figure) differs from one amino acid to another. These side chains polypeptide chain(s). This sequence of amino acids determines the
can vary in size from just one hydrogen atom in glycine to a large higher levels of protein structure and is encoded in genes.
heterocyclic group in tryptophan. The variable side chain gives each A protein's secondary structure consists of regularly repeating local
amino acid unique properties. The side chains can also characterize the structures stabilized by hydrogen bonding between the carboxylic and
amino acid as (1) nonpolar or hydrophobic, (2) neutral (uncharged) but amino groups of the backbone. The most common secondary

3.7.1 https://bio.libretexts.org/@go/page/17000
 structures include the alpha-helix and beta-sheet. Because secondary
structures are local, many regions of different secondary structures can
be present in the same protein molecule.
A protein's tertiary structure refers to the overall three-dimensional
shape of a single protein molecule. It is determined by the spatial
relationship of non-covalent and covalent bonds between the "R"
groups of distant amino acids in a polypeptide. The tertiary structure is
what controls the basic function of the protein.
Not all proteins have a final, quaternary structure. This is a structure
formed by several protein molecules that function together as a single
protein complex.

Figure 3.7.5 : Myoglobin is a protein found in the muscle tissues of most

mammals. It binds with oxygen to supply the cells with this element. The
modle shows the 3D structure of the protein.
The chief characteristic of proteins that allows their diverse set of
functions is their ability to bind other molecules specifically and tightly.
For example, myoglobin can bind specifically and tightly with oxygen.
The region of a protein responsible for binding with another molecule is
known as the binding site. This site is often a depression on the
molecular surface, determined largely by the tertiary structure of the
protein.

PROTEIN CONSUMPTION, DIGESTION, AND

SYNTHESIS
Proteins are necessary for the diets of humans and other animals. We
cannot make all the different amino acids we need, so we must obtain
some of them from the foods we consume. Through the process of
Figure 3.7.4 : The levels of structure of a protein called hemoglobin. digestion, we break down the proteins in food into free amino acids that
can then be used to synthesize our own proteins. Protein synthesis from
FUNCTIONS OF PROTEINS amino acid monomers takes place in all cells and is controlled by genes.
The diversity of protein structures explains how this class of biochemical Once new proteins are synthesized, they generally do not last very long
compounds can play so many important roles in living things. What are before they are degraded and their amino acids are recycled. A protein's
the roles of proteins? lifespan is generally just a day or two in mammalian cells.
Some proteins have structural functions. They may help cells keep
REVIEW
their shape or make up muscle tissues.
1. What are proteins?
Many proteins are enzymes that speed up chemical reactions in cells.
2. How do two amino acids combine together to make a dipeptide?
Enzymes are usually highly specific and accelerate only one or a few
3. Outline the four levels of protein structure.
chemical reactions. Thousands of different biochemical reactions are
4. Identify four functions of proteins.
known to be catalyzed by enzymes, including most of the reactions
5. Explain why proteins can take on so many different functions in living
involved in metabolism. A reaction without an enzyme might take
things.
millions of years to complete, whereas, with the proper enzyme, it
6. What is the role of proteins in the human diet?
may take just a few milliseconds!
7. Can you have a protein with both an alpha helix and a beta-sheet?
Other proteins are antibodies. These are proteins that bind to specific
Why or why not?
foreign substances, such as proteins on the surface of bacterial cells.
8. If there is a mutation in a gene that causes a different amino acid to be
This targets the cells for destruction.
encoded than the one that is usually encoded in that position within
Still, other proteins carry messages or materials. For example, a
the protein, would that affect:
protein called myoglobin is an oxygen-binding protein found in the
muscle tissues of most mammals including humans. You can see a A. The primary structure of the protein? Explain your answer.
model of the tertiary structure of myoglobin in the figure below. B. The higher structures (secondary, tertiary, quaternary) of the
protein? Explain your answer.
C. The function of the protein? Explain your answer.
9. What is the region of a protein responsible for binding to another
molecule called? Which level/s of protein structure create this region?
10. Arrange the following in order from the smallest to the largest level of
organization:
11. peptide; protein; amino acid; polypeptide

3.7.2 https://bio.libretexts.org/@go/page/17000
12. True or False. You can tell the function of all proteins from their 2. Amino acid by YassineMrabet, public domain via Wikimedia
quaternary structure. Commons
13. Explain what the reading means when it says that amino acids are 3. Peptide formation by YassineMrabet, public domain via Wikimedia
“recycled.” Commons
https://bio.libretexts.org/link?17000#Explore_More 4. Peptide bond by OpenStax, CC BY 3.0 via Wikimedia Commons
5. Myoglobin by AzaToth, public domain via Wikimedia Commons
ATTRIBUTIONS 6. Text adapted from Human Biology by CK-12 licensed CC BY-NC 3.0
1. Protein Shake by Sandstein, licensed CC BY 3.0 via Wikimedia
This page titled 3.7: Proteins is shared under a CK-12 license and was authored,
Commons
remixed, and/or curated by Suzanne Wakim & Mandeep Grewal via source
content that was edited to the style and standards of the LibreTexts platform.

3.7.3 https://bio.libretexts.org/@go/page/17000