The folding of many newly synthesized proteins in the cell depends on a set of conserved
proteins known as molecular chaperones. These prevent the formation of misfolded protein …

The unifying feature of all proteins that are transported out of the cytoplasm of gram-negative
bacteria by the general secretory pathway (GSP) is the presence of a long stretch of …

PERMISSIVENESS of the host cell to productive infection by onco-retroviruses is cell-cycle
dependent1, and nuclear localization of viral nucleoprotein preintegration complexes will …

Recently, we documented that the short, proline-rich antibacterial peptides pyrrhocoricin,
drosocin, and apidaecin interact with the bacterial heat shock protein DnaK, and peptide …

Heat shock proteins (Hsps) were first identified as proteins whose synthesis was enhanced
by stresses such as an increase in temperature. Recently, several of the major Hsps have …

Functional proteins within cells are normally present in their native, completely folded form.
However, vital processes of protein biogenesis such as protein synthesis and translocation …

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 …

Molecular chaperones of the Hsp70 class bind unfolded polypeptide chains and are thought
to be involved in the cellular folding pathway of many proteins. DnaK, the Hsp70 protein of …

Membrane and secretory proteins cotranslationally enter and are folded in the endoplasmic
reticulum (ER). Misfolded or unassembled proteins are discarded by a process known as ER …

Molecular chaperones of the Hsp70 type transiently sequester unfolded segments of
proteins and promote their correct folding. Target peptides were labeled with an …