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POINT ONE (WHAT ARE THE TYPES OF NON-COVALENT INTERACTIONS PRESENT IN PROTEIN MOLECULES?)

Non-covalent interactions are the types of bonds that are not as strong as covalent bonds although they can affect the structure and the function of the protein molecule.

These interactions include hydrogen bonds in which the main atom is hydrogen that shows a partial positive charge and binds to an electronegative atom such as an oxygen or nitrogen atom.

Other interactions include ionic interactions, hydrophobic interactions that can be seen between the hydrophobic amino acid residues present in the protein chain, and the weak Van der Waals interactions.

These are the four major non-covalent interactions that can be spotted within protein molecules.

POINT TWO (HYDROGEN BONDS)

As have been stated above, these bonds are mainly seen in the secondary, tertiary and quaternary configuration of the protein molecules. In the case of secondary structure, there is formation of alpha helical and beta-sheets that shows presence of hydrogen bond interactions that provided rigidity and stability to the overall structure.

A peptide is a polymeric sequence that is made up of individual units of amino acids and the bond linking these units is the peptide bond. The amino acid residues of a single chain can interact with other amino acid residues in the same peptide chain (intrachain bonds) and these allows the peptide to undergo changes in their conformation through bends and folds.

Tertiary structure is mainly associated with the process of folding of the peptide chain. This too involves the presence of hydrogen bonds that support covalent interactions like disulfide bonds to bring about proper folding of the protein structure to maintain its functional state.

Quaternary structure too shows interactions in the form of hydrogen bonds between different peptide subunits and these interactions helps in improving the stability of the protein molecule.

POINT THREE (HYDROPHOBIC INTERACTIONS)

There are certain amino acids that shows presence of hydrophobic side chains (that do not show affinity towards water molecules One such amino acid is valine.

Interactions between these amino acids are mainly found in the tertiary structure of the protein molecule and even if these are weak interactions, they help in clumping the hydrophobic amino acid residues near the central part of the protein molecule and thus helps in providing a configuration stability to the protein structure.

POINT FOUR (Van der Waals interactions)

In this case, we are dealing with the dipole interactions that are induced depending upon the presence of different amino acids in associated with other amino acids. We can consider similar examples of hydrophobic interactions mentioned above.

These are weak interactions and persist for a limited time period and mainly are associated with maintaining the secondary structures.

POINT FIVE (IONIC INTERACTIONS)

In this case, we have to consider the charged groups associated with the amino acids. These include amino group as well as the carboxyl group depending upon the pH of the surrounding medium.

These groups interact with each other and form stable linkages mainly found in the tertiary structures and the quaternary structures of the protein molecule. In simple terms, there is association between a positively charged group of one protein molecule and a negatively charged group of another protein molecule.