Actin is one of the most abundant proteins in nature. It is found in all eukaryotes and plays a
fundamental role in many diverse and dynamic cellular processes. Also, actin is one of the …

Partially folded conformations are important players in protein self-organization, function,
and misfolding, thus attracting the intensive and constant attention of researchers. Different …

Abstract GdmCl‐, urea‐, and pH‐induced unfolding pathways of bovine carbonic anhydrase
II have been analyzed by using changes induced by different denaturing agents in intensity …

In addition to the well-known monomeric globular (G-actin) and polymeric fibrillar (F-actin)
forms, actin can exist in the so-called inactivated form (I-actin). Hsp70 chaperon, prefoldin …

A free-energy-based approach is used to describe the mechanism through which
chaperonin-containing TCP-1 (CCT) folds the filament-forming cytoskeletal protein actin …

In this work actin is used to illustrate connection of protein fluorescence characteristics with
its structure. On one hand, it has been demonstrated what kind of information about the …

About 30% of proteins require cofactors for their proper folding. The effects of cofactors on
the folding reaction have been investigated with α‐lactalbumin as a model protein and metal …

The kinetics of actin unfolding induced by guanidine hydrochloride of different
concentrations was studied. The parametric representation of the kinetic dependencies of …

The 36 kDa fragment of actin molecule obtained with the protease from E. coli A2 strain
[(1988) FEBS Lett. 228, 172] was shown to begin with Val-43 and retain the COOH-terminal …

The kinetics of actin unfolding induced by guanidine hydrochloride has been studied. On the
basis of obtained experimental data a new kinetic pathway of actin unfolding was proposed …