Different types of proteins. The structure and properties of amino acids. Formation of peptide bonds.
We tend to think of protein as a mass noun: a homogeneous substance, something that your diet should contain in a certain proportion. But if you ever work in a molecular biology lab (say, for a summer internship), protein may start to look very different to you.
How so? Well, you may see firsthand that protein isn’t just a single substance. Instead, there are lots and lots of different proteins in an organism, or even in a single cell. They come in every size, shape, and type you can imagine, and each one has a unique and specific job. Some are structural parts, giving cells shape or helping them move. Others act as signals, drifting between cells like messages in a bottle. Still others are metabolic enzymes, putting together or snapping apart biomolecules needed by the cell. And, odds are, one of these unique molecular players will become yours for the duration of your research!
Proteins are among the most abundant organic molecules in living systems and are way more diverse in structure and function than other classes of macromolecules. A single cell can contain thousands of proteins, each with a unique function. Although their structures, like their functions, vary greatly, all proteins are made up of one or more chains of amino acids. In this article, we will look in more detail at the building blocks, structures, and roles of proteins.
Types and functions of proteins
Proteins can play a wide array of roles in a cell or organism. Here, we’ll touch on a few examples of common protein types that may be familiar to you, and that are important in the biology of many organisms (including us).
Enzymes act as catalysts in biochemical reactions, meaning that they speed the reactions up. Each enzyme recognizes one or more substrates, the molecules that serve as starting material for the reaction it catalyzes. Different enzymes participate in different types of reactions and may break down, link up, or rearrange their substrates.
One example of an enzyme found in your body is salivary amylase, which breaks amylose (a kind of starch) down into smaller sugars. The amylose doesn’t taste very sweet, but the smaller sugars do. This is why starchy foods often taste sweeter if you chew them for longer: you’re giving salivary amylase time to get to work.
Hormones are long-distance chemical signals released by endocrine cells (like the cells of your pituitary gland). They control specific physiological processes, such as growth, development, metabolism, and reproduction. While some hormones are steroid-based (see the article on lipids), others are proteins. These protein-based hormones are commonly called peptide hormones.
For example, insulin is an important peptide hormone that helps regulate blood glucose levels. When blood glucose rises (for instance, after you eat a meal), specialized cells in the pancreas release insulin. The insulin binds to cells in the liver and other parts of the body, causing them to take up the glucose. This process helps return blood sugar to its normal, resting level.
Some additional types of proteins and their functions are listed in the table below:
Protein types and functions
|Digestive enzyme||Amylase, lipase, pepsin||Break down nutrients in food into small pieces that can be readily absorbed|
|Transport||Hemoglobin||Carry substances throughout the body in blood or lymph|
|Structure||Actin, tubulin, keratin||Build different structures, like the cytoskeleton|
|Hormone signaling||Insulin, glucagon||Coordinate the activity of different body systems|
|Defense||Antibodies||Protect the body from foreign pathogens|
|Contraction||Myosin||Carry out muscle contraction|
|Storage||Legume storage proteins, egg white (albumin)||Provide food for the early development of the embryo or the seedling|
Proteins come in many different shapes and sizes. Some are globular (roughly spherical) in shape, whereas others form long, thin fibers. For example, the hemoglobin protein that carries oxygen in the blood is a globular protein, while collagen, found in our skin, is a fibrous protein.
A protein’s shape is critical to its function, and, as we’ll see in the next article, many different types of chemical bonds may be important in maintaining this shape. Changes in temperature and pH, as well as the presence of certain chemicals, may disrupt a protein’s shape and cause it to lose functionality, a process known as denaturation.
Amino acids are the monomers that make up proteins. Specifically, a protein is made up of one or more linear chains of amino acids, each of which is called a polypeptide. (We'll see where this name comes from a little further down the page.) There are
types of amino acids commonly found in proteins.
Amino acids share a basic structure, which consists of a central carbon atom, also known as the alpha (α) carbon, bonded to an amino group (
), a carboxyl group ( ), and a hydrogen atom.
Although the generalized amino acid shown above is shown with its amino and carboxyl groups neutral for simplicity, this is not actually the state in which an amino acid would typically be found. At physiological pH (
), the amino group is typically protonated and bears a positive charge, while the carboxyl group is typically deprotonated and bears a negative charge.
Every amino acid also has another atom or group of atoms bonded to the central atom, known as the R group, which determines the identity of the amino acid. For instance, if the R group is a hydrogen atom, then the amino acid is glycine, while if it’s a methyl (
) group, the amino acid is alanine. The twenty common amino acids are shown in the chart below, with their R groups highlighted in blue.
The properties of the side chain determine an amino acid’s chemical behavior (that is, whether it is considered acidic, basic, polar, or nonpolar). For example, amino acids such as valine and leucine are nonpolar and hydrophobic, while amino acids like serine and glutamine have hydrophilic side chains and are polar. Some amino acids, such as lysine and arginine, have side chains that are positively charged at physiological pH and are considered basic amino acids. (Histidine is sometimes put in this group too, although it is mostly deprotonated at physiological pH.) Aspartate and glutamate, on the other hand, are negatively charged at physiological pH and are considered acidic.
A few other amino acids have R groups with special properties, and these will prove to be important when we look at protein structure:
- Proline has an R group that’s linked back to its own amino group, forming a ring structure. This makes it an exception to the typical structure of an amino acid, since it no longer has the standard NH
amino group. If you think that ring structure looks a little awkward, you’re right: proline often causes bends or kinks in amino acid chains.
- Cysteine contains a thiol (-SH) group and can form covalent bonds with other cysteines. We'll see why this is important to protein structure and function in the article on orders of protein structure
Finally, there are a few other “non-canonical” amino acids that are found in proteins only under certain conditions.
Each protein in your cells consists of one or more polypeptide chains. Each of these polypeptide chains is made up of amino acids, linked together in a specific order. A polypeptide is kind of like a long word that is "spelled out" in amino acid letters
. The chemical properties and order of the amino acids are key in determining the structure and function of the polypeptide, and the protein it's part of. But how are amino acids actually linked together in chains?
The amino acids of a polypeptide are attached to their neighbors by covalent bonds known as a peptide bonds. Each bond forms in a dehydration synthesis (condensation) reaction. During protein synthesis, the carboxyl group of the amino acid at the end of the growing polypeptide chain chain reacts with the amino group of an incoming amino acid, releasing a molecule of water. The resulting bond between amino acids is a peptide bond
Because of the structure of the amino acids, a polypeptide chain has directionality, meaning that it has two ends that are chemically distinct from one another. At one end, the polypeptide has a free amino group, and this end is called the amino terminus (or N-terminus). The other end, which has a free carboxyl group, is known as the carboxyl terminus (or C-terminus). The N-terminus is on the left and the C-terminus is on the right for the very short polypeptide shown above.
How do we go from the amino acid sequence of a polypeptide to the three-dimensional structure of a mature, functional protein? To learn how interactions between amino acids cause a protein to fold into its mature shape, I highly recommend the video on orders of protein structure.
Want to join the conversation?
- N-terminus and C-terminus. What terminates extension of peptide linkage? Are they guaranteed not to react with other amino acids? If so how?...is it like how there aren't any random amino acids beside those 23 mentioned above, because i.e. for Lynsine, any more hydrocarbon backbone added to the hydrocarbon backbone of lynsine makes it unstable and is actually impossible or something?
And would they be in zwitterion at physiological pH? Could this be why the terminus ARE terminus?(13 votes)
- To answer your first question, you need to look at the process of creating a peptide during Translation in the Ribosome. Messenger RNA is a sequence of nucleotides, three nucleotides is a codon, and codons code (go figure) for certain amino acids, codons also code a "start" and "stop". So in a example the ribosome will read a start codon and start building a peptide until it reaches a stop codon. There is your termination. I'm not sure how to explain the reasons for the differences in the 23 amino acids. Ribosomes are almost like computers robotically doing what the inputted code commands it to do.
Also, I wanted to add that this isn't the end of the story. Things happen to the peptides after transcription within the cell. For example, insulin isn't transcribed fully functional but has to undergo several processes (cutting of pieces, adding) within the cell before it lives up to it's essential functions.(14 votes)
- how are proteins and phenotypes related to one another(5 votes)
- Provided that a protein has been transcribed and translated or "expressed" by the genes, that is the direct expression of phenotype. Large scale that may be seen in an organism as eye color, hair color, etc., as each protein has a different function.(7 votes)
- Should I make any distinction between the qualities: non-polar and hydrophobic or polar and hydrophilic? Can I use these terms interchangeably; which is to say, am I allowed to say non-polar instead of hydrophobic?(5 votes)
- Yes, you should make a distinction. While it is definitely true that most of the time they are the same, it is a good idea to keep in mind the individual definitions of polar, non-polar, hydrophobic, and hydrophilic.(6 votes)
- In the amino acid table, the proline is throwing me off. Isn't proline nonpolar?(6 votes)
- I too agree with this. Proline is nonpolar and aliphatic according to my textbook as well as on wikipedia and plenty of other sources. I mean it makes sense, it's just a cyclic side chain!(0 votes)
- Hi, I remember that in the lipids lesson it said that a specific macromolecule (I don´t remember its name) was considered to be a lipid just because it was hydrophobic and in this article, I found this: "For example, amino acids such as valine and leucine are nonpolar and hydrophobic." So my question is what is the difference between the other macromolecule that was called a lipid because of its being hydrophobic and these proteins?(5 votes)
- It is the presence of amine group and a carboxylic group with a specific configuration that makes a macro molecule to be classified as an amino acid. If you watch the video again, I am sure you would understand.(5 votes)
- If enzymes are proteins, and they can function as a part of the digestive system, doesn't that mean that the enzymes will be breaking down other proteins in the eaten food? So proteins can break down other proteins?(4 votes)
- Do ribosomes make amino acids or do they just synthesize proteins? If so, where are amino acids made?(2 votes)
- No, ribosomes don't make amino acids. They are just the sites where amino acids get linked together to form polypeptides.
Of the 20 amino acids, 9 are essential, i.e, cannot be made by our body. We obtain them from the food we eat. The protein in the food is digested and broken down to release the amino acids. The essential amino acids are :
The remaining amino acids are non-essential, i.e, they can be produced by our body. They are produced by modifications of some of the essential amino acids. For example, Tyrosine is produced from Phenylalanine. This process occurs in the cytoplasm of cells, but it can also occur in the mitochondria as some enzymes and reactants (like alpha-keto glutarate) are found there.(3 votes)
- In the picture with the peptide bonding near the end, why are the hydrogens replaced with "R" groups?(2 votes)
- Distinguish between proteins and amino acids(2 votes)
- "Some amino acids, such as lysine and arginine, have side chains that are positively charged at physiological pH and are considered basic amino acids"
"Aspartate and glutamate, on the other hand, are negatively charged at physiological pH and are considered acidic"
What is going on? Positive charge means that it has excess of H+ protons, so why is it basic and vice versa?(2 votes)
- Lysine and arginine accept a proton and, in so doing, they act as bases and become positively charged. (Compare them with ammonia, which is a base and which becomes protonated in water to give NH4+ and OH- ions.)
Aspartate and glutamate, on the other hand, lose protons and become negatively charged. They act as acids. (Compare them with acetic acid, which dissociates in water to give acetate ions and H3O+.)(2 votes)