| Outcomes: In this article I will be discussing about | | | | structure of a protein it is not completely possible to |
| proteins and its structure. | | | | predict the entire structure of a protein accurately |
| WHAT ARE PROTEINS? | | | | just from the sequence |
| Proteins are a kind of macromolecules which mostly | | | | Two types of folding motifs can be seen in a |
| executes the genetically instructed programs and | | | | secondary structure they are 1. Alpha helix: It is |
| tasks which takes places both inside and outside of | | | | mainly characterised by hydrogen bonds along the |
| the cells, tissues and even organisms. | | | | chains. Hydrogen bonds between the chains help to |
| Proteins are determined in the form of primary, | | | | form the helix in the protein chain. The presence of |
| secondary and tertiary and quaternary structures. | | | | some amino acids like alanine, aspartic acid glutamic |
| Primary Structure: | | | | acid and leucine favours the alpha helix formation. |
| Proteins are the type of polymers which are formed | | | | The presence of amino acids like proline and glycine |
| from alpha-amino carboxylic acids which is also known | | | | disrupt the alpha helix formation. Because of this |
| as amino acids. | | | | disruption of alpha helix it leads to the folding of |
| All the amino acids have amino group (+H3N) and a | | | | protein molecules. |
| carboxyl group (Coo)-. These both amino and the | | | | BETA SHEETS: |
| carboxyl group are attached to the central atom (H) | | | | These are the parallel/antiparellel sheets. Parallel beta |
| Mostly amino acids differ from each other depending | | | | sheet: In this the peptide chains which are adjacent |
| upon the side group attached to central carbon atom | | | | to each other proceeds in the same direction i.e., (in |
| Secondary Structure: | | | | the direction of N-terminal to C-terminal ends in the |
| In the secondary structure bond lengths and bond | | | | same direction.) Anti -parallel sheets: In this type of |
| angles don't vary much. | | | | sheets the adjacent peptide chains proceeds in the |
| In proteins with similar function may typically have | | | | opposite direction to the parallel sheets. |
| the same type of structure. | | | | TERTIARY STRUCTURE: |
| The proteins which have similar structure tend to be | | | | It is the 3-dimensional structure of a polypeptide |
| more conserved than the exact sequence of the | | | | chain of a protein molecule. The secondary structures |
| amino acids. | | | | fold themselves which leads to the formation of |
| Even though the sequence helps to determine the | | | | these tertiary structures. |