Protein Structure: A Brief Analysis
Creating a protein drug is not an easy task to accomplish. Without a clear understanding of the nature of protein structure, you will not be able to make anything but a damaging drug. Many medicine experts believe that studying the protein structure will not only help in formulating a protein drug but also it will help people in understanding the importance of having an adequate level of protein in their body.
This is why we are going to explain the protein structure in brief. So, let us start reading and gain a brief insight into protein structure.
What is a Protein Structure?
Typically, the proteins consist of polymers of amino acids, which are combined by peptide bonds. All proteins on earth are made of 20 different types of amino acids. Every one of these amino acids includes a core design. This design is composed of a central carbon, which is known as ‘alpha carbon.’ This carbon is bonded to the following elements –
- Hydrogen and a carboxyl group
- An amino group and an exclusive side chain or R-group
- Protein Structure – The Features
There are four types of protein structure, and each of the structure has the following functions –
- Primary structure: The main structure includes the linear arrangement of amino acids in protein. It is also the location of covalent bondages like as disulfide bonds between amino acids
- Secondary structure: The secondary structure’s elements stay in the folded or convoluted areas within the protein. A prime example of this can be alpha helices and pleated sheets.
- Tertiary structure: This is the last three-dimensional structure of protein. This structure includes several non-covalent relations between amino acids.
- Quaternary structure: This protein structure is different and includes non-covalent interactions. These interactions combine various polypeptides into a single and big protein.
How To Analyze The Protein Structures?
You can examine different protein structures with the following techniques and equipment –
- An Amino Acid Analyzer
- Peptide mapping and utilization of Edman degradation or mass spectroscopy (for analyzing the sequence)
- Circular Dichroism Spectroscopy (CD) (for analyzing secondary structure)
- Using X-ray crystallography or Nuclear Magnetic Resonance (NMR) analysis (for analyzing three-dimensional structure of protein)