<p> Complementation assays were carried out in a strain of <i>E. coli</i>, MGM100, in which expression of endogenous chaperonins (GroEL-GroES) was under strict control of the pBAD promoter. (A) Various controls for the <i>in vivo</i> system at the indicated growth conditions (10<sup>−2</sup> dilution shown). (B and C) Ten-fold-serial dilutions (10<sup>−2</sup> to 10<sup>−7</sup> shown) of <i>E. coli</i> strain MGM100 harboring plasmid pOFX containing GroEL and the indicated co-chaperonin, grown on agar plates in the presence of glucose and IPTG, but no arabinose: B) at 30°C C) at 44°C.</p
AbstractThe quantitative contribution of chaperonin GroEL to protein folding in E. coli was analyzed...
GroESL is an essential bacterial chaperone system comprising the homotetradecameric, double ring G...
<p>MDH refolding was carried out by either (A) GroEL or (B) Cpn60αβ, as described in <a href="http:/...
<p>(A) Examination of the <i>in vivo</i> system at the indicated growth conditions. (B) Ten-fold-ser...
Human malaria is among the most ubiquitous and destructive tropical, parasitic diseases in the world...
As the GroES/GroEL chaperonin system is the only bacterial chaperone that is essential under all con...
Cochaperonins (cpn10) assist chaperonins (cpn60) in promoting folding and assembly of other proteins...
Brassica napus chaperonin-60 alpha and chaperonin-60 beta genes expressed separately and in combinat...
As the GroES/GroEL chaperonin system is the only bacterial chaperone that is essential under all con...
Over-expression of the chaperonins GroEL and GroES significantly suppressed the temperature-dependen...
A series of COOH-terminal deletions of the chaperonin GroEL have been examined for effects in vivo a...
AbstractOver-expression of the chaperonins GroEL and GroES significantly suppressed the temperature-...
Molecular chaperones play an integral role in the folding of most polypeptides in vivo, and protect ...
pET11a AmpR the E. coli groES gene inserted at the NdeI and BamHI sites (pT7-ES), pET11a AmpR the E....
<p>MDH refolding was carried out by either (A) GroEL or (B) Cpn60αβ, as described in <a href="http:/...
AbstractThe quantitative contribution of chaperonin GroEL to protein folding in E. coli was analyzed...
GroESL is an essential bacterial chaperone system comprising the homotetradecameric, double ring G...
<p>MDH refolding was carried out by either (A) GroEL or (B) Cpn60αβ, as described in <a href="http:/...
<p>(A) Examination of the <i>in vivo</i> system at the indicated growth conditions. (B) Ten-fold-ser...
Human malaria is among the most ubiquitous and destructive tropical, parasitic diseases in the world...
As the GroES/GroEL chaperonin system is the only bacterial chaperone that is essential under all con...
Cochaperonins (cpn10) assist chaperonins (cpn60) in promoting folding and assembly of other proteins...
Brassica napus chaperonin-60 alpha and chaperonin-60 beta genes expressed separately and in combinat...
As the GroES/GroEL chaperonin system is the only bacterial chaperone that is essential under all con...
Over-expression of the chaperonins GroEL and GroES significantly suppressed the temperature-dependen...
A series of COOH-terminal deletions of the chaperonin GroEL have been examined for effects in vivo a...
AbstractOver-expression of the chaperonins GroEL and GroES significantly suppressed the temperature-...
Molecular chaperones play an integral role in the folding of most polypeptides in vivo, and protect ...
pET11a AmpR the E. coli groES gene inserted at the NdeI and BamHI sites (pT7-ES), pET11a AmpR the E....
<p>MDH refolding was carried out by either (A) GroEL or (B) Cpn60αβ, as described in <a href="http:/...
AbstractThe quantitative contribution of chaperonin GroEL to protein folding in E. coli was analyzed...
GroESL is an essential bacterial chaperone system comprising the homotetradecameric, double ring G...
<p>MDH refolding was carried out by either (A) GroEL or (B) Cpn60αβ, as described in <a href="http:/...