The chaperone system formed by DnaK, DnaJ and GrpE mediates stress‐dependent negative
modulation of the Escherichia coli heat shock response, probably through association …

… and folding properties allows mechanistic dissection of the assisted folding pathways (RNase
T1, CheY, catabolite activator protein, FtsA, ribosomal protein L2 and proOmpA of E.coli; S.…

… in total soluble extracts of [ 35 S]methionine‐labeled wild‐type cells (… We performed a
seeding experiment in which [ 35 S]… [ 35 S]methionine‐labeled cell extracts were incubated for 5 …

… The initial association rate (over the first 150 s) was estimated by fitting a linear equation
to data (BIAEVALUATION 3.1, BIAcore AB, Uppsala, Sweden). The data were analyzed …

Determination of the structure of the substrate binding domain of the Escherichia coli Hsp70
chaperone, DnaK, and the biochemical characterisation of the motif it recognizes within …

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The 70 kDa heat shock proteins (the Hsp70 family) assist refolding of their substrates through
ATP-controlled binding. We have analyzed mutants of DnaK, an Hsp70 homolog, altered …

… It is essential to determine Hsp90’s substrate-binding site to reveal the molecular principles
of … However, Hsp90’s affinity for Tau in the ATP state did not differ significantly from the affinity …

Inorganic materials having high surface areas are of interest, for example, in heterogeneous
catalysis where the activity of a catalyst depends largely on its surface.[1] Metal oxides with …

The Hsp70 chaperone activity in protein folding is regulated by ATP-controlled cycles of
substrate binding and release. Nucleotide exchange plays a key role in these cycles by …