2+ Year Member
May 22, 2016
Medical Student (Accepted)
Does anyone know is a reducing condition reagent such as "mercatenphenol" or whatever it is called will ALSO denature a protein fully when there is no heat, detergent or altered PH involved. What happens when a protein is simply subjected to reducing conditions.... do only disulfide bonds get affected while the rest of the protein is okay.


2+ Year Member
Nov 1, 2015
Medical Student
It depends on the protein but in general, the protein will have disulfides reduced and be fine otherwise. So the intracellular environment is actually very reducing and proteins that function in this environment must be able to tolerate reducing conditions. Similarly, the extracellular environment is very oxidizing and thus proteins that are exposed to the exterior must be able to tolerate oxidizing conditions.

In order to denature a protein, you need to replace the favorable interactions with even more favorable ones - it's a simple thermodynamic argument. Unless the unfolded form is stabilized vis-a-vis the folded form, the latter will remain the thermodynamically-favored product.