Hi Jordan, The minimization energy is not meant to be used quantitatively as the stability of a structure. Minimization just goes to nearby local minimum, whereas the stability is really a free energy of a huge ensemble of structures (in solution) in folded states vs. unfolded states of the same sequence. To summarize, if you want to figure out the relative stability of mutants, you will have to use some other program/method than Chimera. I hope this helps, Elaine ----- Elaine C. Meng, Ph.D. UCSF Chimera(X) team Department of Pharmaceutical Chemistry University of California, San Francisco

On Aug 17, 2020, at 10:18 AM, Jordan Harriman <jnharrim@iu.edu> wrote:

Hi there, I have a protein I'm modifying, for a total of 28 unique mutations. My question is if it's possible to tell the energetic difference between a minimized structure vs. an unminimized structure. Following that, if it's possible to rank minimized structures in terms of greatest stability. Is there some quantifiable output I can use to compare structures? Best, Jordan