Editing Protein structure (section)

== Protein stability ==
{{main|Equilibrium unfolding}}
Thermodynamic stability of proteins represents the [[Gibbs free energy|free energy difference]] between the folded and [[Denaturation (biochemistry)|unfolded]] protein states. This free energy difference is very sensitive to temperature, hence a change in temperature may result in unfolding or denaturation. [[Denaturation (biochemistry)|Protein denaturation]] may result in loss of function, and loss of native state. The free energy of stabilization of soluble globular proteins typically does not exceed 50 kJ/mol.{{Cn|date=August 2018}} Taking into consideration the large number of hydrogen bonds that take place for the stabilization of secondary structures, and the stabilization of the inner core through hydrophobic interactions, the free energy of stabilization emerges as small difference between large numbers.<ref>{{cite journal | vauthors = Jaenicke R | title = Protein structure and function at low temperatures | journal = Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences | volume = 326 | issue = 1237 | pages = 535–553 | date = January 1990 | pmid = 1969647 | doi = 10.1098/rstb.1990.0030 | doi-access = free | jstor = 2398703 | bibcode = 1990RSPTB.326..535J }}</ref>