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 …

This review summarizes experimental data illuminating the mechanism of suppression of
heat-induced protein aggregation by α-crystallin, one of the small heat shock proteins. The …

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

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 …

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 …

We report here that in vitro exposure of monomeric actin to hydrogen peroxide leads to a
conversion of 6 of the 16 methionine residues to methionine sulfoxide residues. Although …

Thermal denaturation and aggregation of rabbit muscle glyceraldehyde-3-phosphate
dehydrogenase (GAPDH) have been studied using differential scanning calorimetry (DSC) …

The effect of Ca2+ on physicochemical and conformational changes of threadfin bream (TB)
myosin and actin during setting at 25 and 40° C was investigated. Ca2+ ion at 10 to 100 mM …

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

Actin is one of the proteins that rely on chaperonins for proper folding. This paper shows that
the thermal unfolding of G‐actin, as studied by CD and ultraviolet difference spectrometry …