Proteins
We generally tend to think of proteins only from a dietary lens, as a component of what we eat. However, they are among the most important and abundant organic macromolecules in the human body, with diverse structures and functions. Every cell contains thousands and thousands of proteins, each with specific functions. Some help in the formation of cellular membrane or walls, some help the cell to move, others act as messages or signals and flow seamlessly from one cell to another, carrying information.
Protein Expression
The method by which living organisms synthesize proteins and further modify and regulate them is called protein expression. Protein expression plays a significant role in several types of research and is highly utilized in molecular biology, biochemistry, and protein research laboratories.
All proteins exist in primary structure and most of them found in secondary, tertiary structure, and quaternary structure of proteins.
The primary structure of proteins has specific amino acids sequence that makes up the protein. Every protein has its own unique amino acid sequence that determines the tertiary structure, and quaternary structure of that protein. The linear polymer of amino acids i.e., primary structure, in which amino acids are held together by peptide bonds (Covalent bond).
After the formation of the primary structure of proteins, the linear polypeptide starts twisting in regular patterns and formed the secondary structure include alpha-helices, beta-pleated sheets that stabilized by hydrogen bonds.
The tertiary structure of the protein formed by the spatial arrangement of amino acids. Since the proteins fold in an aqueous environment and tertiary structure stabilized by an ionic bond between charged amino acid sequence, hydrophobic interaction (Van der Waals force) between the non-polar side chain of amino acid sequence and disulfide bond (Covalent bond).
Larger proteins consist of two or more polypeptide chains that have a fourth level of a structure called quaternary structure proteins. These subunits are stabilized by non-covalent interactions or covalent bonds i.e. disulfide bonds.
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