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Table of Contents
Introduction
Amino acids are the building blocks of proteins. When food containing protein is digested, amino acids are the final product. After being absorbed, these amino acids are used by cells in the body to create chemicals and structures required for life.
There are 21 different amino acids. Amino acids each consist of:1
- An amino group: -NH2+
- A carboxylate group: -CO2-
- An “R” side chain which is specific to that amino acid
Classes of amino acids
Amino acids can be grouped into four different classes based on their “R” side chains (Figure 1):1
- Polar, charged: hydrophilic
- Polar, uncharged: hydrophilic
- Special cases: hydrophilic
- Non-polar, uncharged: hydrophobic

Protein structure
In order to form a protein, amino acids link together and fold into their final functional unit.
There are four levels of structure that relate to the complexity of the formation (Figure 2):2
- Primary structure: the bonds that form between each amino acid, known as peptide bonds
- Secondary structure: the formation of hydrogen bonds between this initial structure
- Tertiary structure: the folding of the peptide chain to form a 3D shape
- Quaternary structure: the linking of multiple polypeptide chains together




Clinical relevance: haemoglobin
Haemoglobin is the protein which carries oxygen around the body in red blood cells. It consists of four globin chains (two alpha and two beta) and four haem groups.
There are several conditions in which this structure is disrupted:2
- Thalassaemia: a range of genetic conditions leading to defects in either the alpha or beta-globin chains. This leads to haemoglobin with suboptimal function, causing the production of abnormal red blood cells
- Sickle cell anaemia: altered beta-globin chain due to a genetic mutation that switches out the amino acid glutamic acid to valine. This leads to a red blood cell with an abnormal shape which causes microvascular occlusion.
Nutrition
Proteins are one of the three major macronutrients in human nutrition (with lipids and carbohydrates the other two).
In humans, protein is critical for the growth, maintenance and structural composition of cells.3
Digestion
During digestion, proteins are broken down into smaller peptide chains in the stomach by reacting with hydrochloric acid and proteases present (Figure 3).
This allows for absorption and the formation of amino acids not able to be made by the body (known as the nine essential amino acids):
- histidine
- isoleucine
- leucine
- lysine
- methionine
- phenylalanine
- threonine
- tryptophan
- valine




Sources of protein
Dietary protein can come from animal and plant sources. Animal sources are known to contain all essential amino acids, whereas plant sources generally are missing lysine.3
Animal sources of protein include:
- Meat (beef, pork, and chicken)
- Eggs
- Fish
Plant sources of protein include:
- Tofu
- Tempeh
- Legumes (lentils, peas, and beans)
- Wholegrains
Protein deficiency
Deficiency in the essential amino acids leads to inhibition of protein synthesis in the body. This leads to deficient growth, upkeep of the immune system, reduced kidney function and reduced organ function.2,3
Protein deficiency is rare in developed regions of the world. Clinical features of protein deficiency may include:
- Oedema
- Faltering growth in children
- Low muscle mass
- Loss of or poor growth of hair
- Chronic exhaustion
The amount of protein a person requires differs from person to person depending on their current health situation. For example, growing children, people who are unwell, and those undertaking large amounts of exercise require more protein.
Key points
- Amino acids are the building blocks for all proteins in the body
- Proteins undergo four stages of folding from a primary chain of amino acids using peptide bonds, to a quaternary multi-protein structure
- Some proteins can be made by the body, but the nine essential amino acids must be consumed as they are unable to be made intrinsically
Editor
Dr Chris Jefferies
References
Reference texts
- Hughes AB. Amino acids, peptides, and proteins in organic chemistry. 2012. Wiley-VCH. Available from [LINK]
- Fry MA. Essential biochemistry for medicine. 2010. Wiley-Blackwell. Available from [LINK]
- Langley-Evans SCA. Nutrition health and disease: a lifespan approach. 2015. John Wiley & Sons, Ltd. Available from [LINK]
Image references
- Figure 1. Dan Cojocari. License: [CC BY-SA 3.0]
- Figure 2. Kep17. License: [CC BY-SA 4.0]
- Figure 3. OpenStax College. License: [CC BY 3.0]