Describe structural changes that can occur to a protein after translation is make it function properly

The structural variations that can happen in a protein after translation to make it function appropriately are:

•Folding – In the cytoplasm it partakes chaperonin protein that will aid to fold the protein into a purposeful shape. The hydrogen bonds will form to create secondary protein and disulfide bonds will form tertiary structure and hydrogen bonds. 

•Cleavage – The activation into a purposeful protein over cleavage of certain amino acid sequences in which the amino acid order can fold to form the secondary or tertiary structure.

•Chemical Modification – A method of chemically responding a protein or nucleic acid with chemical components. 

•Elaboration – In particulars of folding, chaperones, kinds of bonds, the role of Golgi, combination into current molecular arrays. Etc.

This is what i found on google“ the monomers combine with each other via covalent bonds to form larger molecules known as polymers. in doing so, monomers release water molecules as byproducts. this type of reaction is known as dehydration synthesis, which means “to put together while losing water. in the process, a water molecule is formed.” i hope this you

Type in the minus sign