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ProteomicsA Proteome-Wide Map of Chaperone-Assisted Protein Refolding in a Cytosol-like Milieu
The journey by which proteins navigate their energy landscapes to their native structures is complex, involving (and sometimes requiring) many cellular factors and processes operating in partnership with a given polypeptide chain’s intrinsic energy landscape. The cytosolic environment and its compl...
ORGANISM(S): Escherichia coli 
2022-11-23 | PXD030869 | Pride
Protein refolding Chaperone refolding Groel/es folding Proteomics 
ProteomicsChaperone Dependency during Primary Protein Biogenesis Does Not Correlate with Chaperone Dependency during in vitro Refolding
Many proteins require molecular chaperones to fold into their functional native forms. Previously we used limited proteolysis mass-spectrometry (LiP-MS) to find that ca. 40% of the E. coli proteome do not efficiently refold spontaneously following dilution from denaturation, a frequency that drops t...
ORGANISM(S): Escherichia coli 
2025-09-22 | PXD064568 | Pride
Chaperones  protein folding  dnak  trigger factor  co-translational folding  structural proteomics 
UnknownChaperone dependency during biogenesis does not correlate with chaperone dependency during refolding.
Not available
S-EPMC12759075 | biostudies-literature
UnknownDodecamer assembly of a metazoan AAA+ chaperone couples substrate extraction to refolding.
Not available
S-EPMC10171807 | biostudies-literature
UnknownA proteome-wide map of chaperone-assisted protein refolding in a cytosol-like milieu.
Not available
S-EPMC9860312 | biostudies-literature
TranscriptomicsGenome-wide measurement of RNA folding energies
RNA structural transitions are important in the function and regulation of RNAs. Here, we reveal a layer of transcriptome organization in the form of RNA folding energies. By probing yeast RNA structures at different temperatures, we obtained relative melting temperatures (Tm) for RNA structures in ...
ORGANISM(S): Saccharomyces cerevisiae 
2012-09-09 | E-GEOD-39680 | biostudies-arrayexpress
UnknownStructural basis for aggregate dissolution and refolding by the Mycobacterium tuberculosis ClpB-DnaK bi-chaperone system.
Not available
S-EPMC8209680 | biostudies-literature
UnknownThe RNA chaperone StpA enables fast RNA refolding by destabilization of mutually exclusive base pairs within competing secondary structure elements.
Not available
S-EPMC8565331 | biostudies-literature
UnknownChaperone Dependency during Primary Protein Biogenesis Does Not Correlate with Chaperone Dependency during <i>in vitro</i> Refolding.
Not available
S-EPMC12224572 | biostudies-literature
UnknownChaperone Dependency during Biogenesis Does Not Correlate with Chaperone Dependency during Refolding
Not available
S-SCDT-10_1038-S44320-025-00166-6 | biostudies-other
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