The properties of protein
It is can be defined as ‘any of numerous organic molecules constituting a large portion of the mass of every life form, composed of 20 or more amino acid linked in one or more long chains, the final shape and other properties of each protein being determined by the side chains of the amino acids and their chemical attachments.
Knowing the function and structure of proteins is crucial for the development of better drugs, higher yields crops, and even synthetic biofuels.
Some proteins are involved in complex biochemical activities. Others contribute to the structure of cells.
Proteins are composed of carbon, hydrogen and nitrogen, and sometimes sulfur and phosphorus. All proteins contain nitrogen at a level of about 16%. The analysis of proteins is determined indirectly by analyzing for protein nitrogen, then multiplying the result by 6.25 to determine the actual amount of protein analyzed.
It is a biological macromolecule composed of a series of smaller, building block molecules called amino acids, linked together in a linear chain, like beads on a string. Different proteins contain different amino acids.
Proteins are joined covalently and non-covalently with other biomolecules including lipids, carbohydrates, nucleic acids, phosphate groups, flavins, heme groups and metal ions. Components such as hemes or metal ions are often called prosthetic groups.
Complexes formed between lipids and proteins are lipoproteins, those with carbohydrates are called glycoproteins, whilst complexes with metal ions lead to metalloproteins.
The hydrophobic effect is the driving forces in the formation of active protein structure. The stability of protein molecules is maintained principally by hydrogen bonding and hydrophobic interactions, which play a crucial role in the formation of the tertiary structure of soluble proteins and oligomeric structure.
This nutrient has a limited life span and constantly undergoes change. The rate of protein turnover varies in different tissues.
The properties of protein
