Protein denaturation

I'm not entirely sure I understand your question. Reversible denaturation of proteins usually involves changing how they fold/crystallize via hydrogen bonding or polar interactions.
For example, the amino acid serine contains an alcohol functionality (-CH2OH) that can hydrogen bond. If one alters the hydrogen bonding by addition of salt, changing pH, heating, etc., a protein that contains a significant amount of Ser will change its crystal structure because the Ser will no longer be "tying it together" in the same way. A changed crystal structure results in changed properties such as solubility, melting temperature, etc., so the protein is said to be "denatured". The process is reversible if the protein reverts to its natural state when the outside influence (salt, heat, etc.) is removed.