what types of bonds or interactions could asparagine form with another amino acid in the chain in order to form a quaternary structure with another protein chain?
Asparagine can form hydrogen bonds polar amino acids to stabilize structure the chain in order to form a quaternary structure with another protein chain.
Since the amide group may absorb two and donate two hydrogen bonds, asparagine has a high potential to form hydrogen bonds.
Both the surface and proteins' inside contain it.
In glycoproteins, asparagine is a frequent location for the attachment of carbohydrates.
Noncovalent connections between adjacent surface hydrophobic and hydrophilic areas on the polypeptide subunits hold the quaternary structure together.
In addition, salt connections can be created by basic and acidic side chains.
As in the tertiary structure, where many polypeptides are bound together to create a single functional unit known as a multimer, the quaternary structure is also stabilised by non-covalent interactions and disulfide bonds.
