Conformational Stability and Dynamics in Crystals Recapitulate Protein Behavior in Solution.

ABSTRACT: A growing body of evidences has established that in many cases proteins may preserve most of their function and flexibility in a crystalline environment, and several techniques are today capable to characterize molecular properties of proteins in tightly packed lattices. Intriguingly, in the case of amyloidogenic precursors, the presence of transiently populated states (hidden to conventional crystallographic studies) can be correlated to the pathological fate of the native fold; the low fold stability of the native state is a hallmark of aggregation propensity. It remains unclear, however, to which extent biophysical properties of proteins such as the presence of transient conformations or protein stability characterized in crystallo reflect the protein behavior that is more commonly stud

SUBMITTER: Sala BM 

PROVIDER: S-EPMC7474178 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature