<p>MDH refolding by either A) GroEL or B) Cpn60αβ was carried out as described in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0113835#s2" target="_blank">Materials and Methods</a> in the presence of increasing concentrations of various co-chaperonin species, as indicated. 100% was taken as the activity of GroEL assisted by a saturating concentration of GroES, or the activity of Cpn60αβ assisted by mt-cpn10. Results are presented as an average of 3 independent experiments ± SD.</p
The proteasome has a crucial part in the degradation of normal, damaged, mutant or misfolded protein...
The proteasome has a crucial part in the degradation of normal, damaged, mutant or misfolded protein...
We have studied how nucleotides (ADP, AMP-PNP, and ATP) and the co-chaperonin GroES influence the Gr...
<p>MDH refolding was carried out by either (A) GroEL or (B) Cpn60αβ, as described in <a href="http:/...
<p>MDH refolding was carried out by either (A) GroEL or (B) Cpn60αβ, as described in <a href="http:/...
<p>Steady-state ATPase activity was measured for each chaperonin. The T.O.N values (1/min) were 3.27...
<p>Refolding of 0.33 µM HCl-denatured MDH by 10 µM of chaperonin GroEL (A), wild-type mHsp60 (B), E3...
<p>Urea-denatured malate dehydrogenase was refolded by GroEL with the help of Pf-cpn20, using At-cpn...
<p>Cpn60β1 oligomer was assembled from monomeric form as described in <a href="http://www.plosone.or...
<p>Refolding of 0.33 µM HCl-denatured MDH by 10 µM of the indicated chaperonin and 20 µM of mHsp10 (...
<p>(A–D) Refolding of 0.33 µM HCl-denatured MDH by 10 µM of the indicated chaperonin and 40 µM of mH...
<p>A binary complex of E321K and HCl-denaturated MDH was pre-incubated for 30 min in the presence of...
<p>Interaction between mHsp10 and different chaperonins was measured using a pulldown assay. 50 µM o...
<p> Complementation assays were carried out in a strain of <i>E. coli</i>, MGM100, in which expressi...
<p>A. Stopped-flow analysis of GroEL CP86-RW upon addition of 1 mM ATP. <i>Black traces</i> correspo...
The proteasome has a crucial part in the degradation of normal, damaged, mutant or misfolded protein...
The proteasome has a crucial part in the degradation of normal, damaged, mutant or misfolded protein...
We have studied how nucleotides (ADP, AMP-PNP, and ATP) and the co-chaperonin GroES influence the Gr...
<p>MDH refolding was carried out by either (A) GroEL or (B) Cpn60αβ, as described in <a href="http:/...
<p>MDH refolding was carried out by either (A) GroEL or (B) Cpn60αβ, as described in <a href="http:/...
<p>Steady-state ATPase activity was measured for each chaperonin. The T.O.N values (1/min) were 3.27...
<p>Refolding of 0.33 µM HCl-denatured MDH by 10 µM of chaperonin GroEL (A), wild-type mHsp60 (B), E3...
<p>Urea-denatured malate dehydrogenase was refolded by GroEL with the help of Pf-cpn20, using At-cpn...
<p>Cpn60β1 oligomer was assembled from monomeric form as described in <a href="http://www.plosone.or...
<p>Refolding of 0.33 µM HCl-denatured MDH by 10 µM of the indicated chaperonin and 20 µM of mHsp10 (...
<p>(A–D) Refolding of 0.33 µM HCl-denatured MDH by 10 µM of the indicated chaperonin and 40 µM of mH...
<p>A binary complex of E321K and HCl-denaturated MDH was pre-incubated for 30 min in the presence of...
<p>Interaction between mHsp10 and different chaperonins was measured using a pulldown assay. 50 µM o...
<p> Complementation assays were carried out in a strain of <i>E. coli</i>, MGM100, in which expressi...
<p>A. Stopped-flow analysis of GroEL CP86-RW upon addition of 1 mM ATP. <i>Black traces</i> correspo...
The proteasome has a crucial part in the degradation of normal, damaged, mutant or misfolded protein...
The proteasome has a crucial part in the degradation of normal, damaged, mutant or misfolded protein...
We have studied how nucleotides (ADP, AMP-PNP, and ATP) and the co-chaperonin GroES influence the Gr...