Proteins are all made of monomers—we knew that word would come in handy—called amino acids. There are 22 different kinds of naturally occurring amino acids, and each one is made of four components:
- A central carbon with one hydrogen
- One carboxyl group (–COOH)
- One amino group (–NH2)
- One R group (–R; Mr. Anonymous is back!)
Amino acids bind to each other by dehydration synthesis: the OH group on one amino acid’s carboxyl group (–COOH) combines with one of the hydrogen groups from another amino acid’s amino group (–NH2). We call the resulting covalent bond a peptide bond. When many amino acids bind together, it’s called a polypeptide.
Watch as we demonstrate the magic of how a peptide bond forms between two amino acids:
To understand how proteins function, we need to understand how they’re put together and what gives them their shape. Proteins actually have four levels of structure with each more complex than the last. As you will soon learn, proteins can either be simple as pie or so high maintenance that you are ready to pull your hair out, which, by the way, is also made of protein.
- Primary structure
- Secondary structure
- Tertiary structure
- Quaternary structure
Secondary structure in proteins results from hydrogen bonds that form between parts of the polypeptide chain that are not variable. By variable, we mean the parts that are not part of the infamous R group. These repeating, nonvariable parts include nitrogens that were originally part of amino groups, now called amides, and the remaining oxygens that are part of carboxyl groups. Both nitrogen and oxygen are somewhat bad at sharing electrons, so they create polar regions. The end result is that the polypeptide has several possible structures: the helix, the sheet, the coil, the loop, and the turn.
While all of this bonding is going on, those R groups aren’t just sitting there twiddling their imaginary thumbs and waiting for something to happen like they were a Redshirt in Star Trek. They are interacting with other R groups, and these interactions give polypeptides their tertiary structure. See what we did there? In reality, secondary and tertiary structure together give a protein it’s three-dimensional (3D) shape. To use a food analogy (since we know how much you love those), a straight line of peas is a good way to think of a polypeptide chain with only primary structure, and a rotini noodle is a good way to think about a polypeptide once it has secondary and tertiary structure. Never mind the fact that both of those foods actually contain mostly carbohydrates.
Some proteins join together in order to carry out their function. The quaternary structure is the overall shape that results once all the interacting subunits of the protein have clumped together. Collagen and hemoglobin are two good examples of proteins with quaternary structure. Read more about their function in our theme on structure and function.
You eat lots of proteins in your diet. Do you ever wonder how they get digested? Special enzymes (read more here) in your gut, called proteases, are able to break down those bonds we just discussed.