Marlena Matuszewska

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The small heat shock proteins are ubiquitous stress proteins proposed to increase cellular tolerance to heat shock conditions. We isolated IbpA, the Escherichia coli small heat shock protein, and tested its ability to keep thermally inactivated substrate proteins in a disaggregation competent state. We found that the presence of IbpA alone during substrate(More)
Small heat shock proteins (sHsps) associate with aggregated proteins, changing their physical properties in such a way that chaperone mediated disaggregation becomes much more efficient. In Escherichia coli two small Hsps, IbpA and IbpB, exist. They are 48% identical at the amino acid level, yet their roles in stabilisation of protein aggregates are quite(More)
Severe thermal stress induces massive intracellular protein aggregation. The concerted action of Hsp70 (DnaK, DnaJ, GrpE) and Hsp100 (ClpB) chaperones results in solubilization of aggregates followed by reactivation of proteins. It was shown that the Hsp70 chaperone system works at the initial step of the disaggregation reaction and is able to disentangle(More)
Addition of hydrazoic acid to alpha,beta-unsaturated aldehydes derived from tri-O-acetyl-D-glucal and -D-galactal gave 3-azido-2,3-dideoxyhexopyranoses. These were converted into 1,4,6-tri-O-acetyl-3-azido-2,3-dideoxyhexopyranoses as well as methyl and ethyl glycosides. Hydrogenation of the proamine group in 3-azido-2,3-dideoxy derivatives provided(More)
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