The effect of additional disulfide bonds on the stability and folding of ribonuclease A.

Abstract excerpt

The significant contribution of disulfide bonds to the conformational stability of proteins is generally considered to result from an entropic destabilization of the unfolded state causing a faster escape of the molecules to the native state. However, the introduction of extra disulfide bonds into proteins as a general approach to protein stabilization yields rather inconsistent results. By modeling studies, we...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Circular Dichroism
• Share to Disulfides
• Share to Enzyme Stability