Autocatalytic Folding of the Folding Catalyst FKBP12

Disabling the folding catalyst is the last critical step in -lytic protease folding

Alpha-Lytic protease ( LP) is an extracellular bacterial pro-protease marked by extraordinary conformational rigidity and a highly cooperative barrier to unfolding. Although these properties successfully limit its proteolytic destruction, thereby extending the functional lifetime of the protease, they come at the expense of foldability (t1/2 1800 yr) and thermodynamic stability (native LP is le...

Osmolyte-Induced Folding and Stability of Proteins: Concepts and Characterization

It is well-known that the typical protein’s three-dimensional structure is relatively unstable in harsh conditions. A practical approach to maintain the folded state and thus improve the stability and activity of proteins in unusual circumstances is to directly apply stabilizing substances such as osmolytes to the protein-containing solutions. Osmolytes as natural occurring organic molecules ty...

Osmolyte-Induced Folding and Stability of Proteins: Concepts and Characterization

It is well-known that the typical protein’s three-dimensional structure is relatively unstable in harsh conditions. A practical approach to maintain the folded state and thus improve the stability and activity of proteins in unusual circumstances is to directly apply stabilizing substances such as osmolytes to the protein-containing solutions. Osmolytes as natural occurring organic molecules ty...

Folding Test Folding Test

Protein Stability, Folding, Disaggregation and Etiology of Conformational Malfunctions

Estimation of protein stability is important for many reasons: first providing an understanding of the basic thermodynamics of the process of folding, protein engineering, and protein stability plays important role in biotechnology especially in food and protein drug design. Today, proteins are used in many branches, including industrial processes, pharmaceutical industry, and medical fields. A...