Chaperone proteins are most notable for the proteo- and cyotoprotective capacities they afford during cellular stress. Under conditions of cellular normalcy, chaperones still play integral roles in the folding of nascent polypeptides into functional entities, in assisting in intracellular/intraorganellar transport, in assembly and maintenance of multi-subunit protein complexes, and in aiding an...

Background. Chaperones and their co-factors are components of a cellular network; they collaborate to maintain proteostasis under normal and harmful conditions. In particular, hsp70 family members and their co-chaperones are essential to repair damaged proteins. Co-chaperones are present in different subcellular compartments, where they modulate chaperone activities. Methods and Results. Our st...

The aim of this study was to assess the use of a chaperone in obstetrical and gynaecological practice in Ireland and to explore patients' opinions. Two questionnaires were designed; one for patients and the other one was sent to 145 gynaecologists in Ireland. One hundred and fifty two women took part in this survey of whom 74 were gynaecological and 78 were obstetric patients. Ninety five (65%)...

In bacteria, ribosome-bound Trigger Factor assists the folding of newly synthesized proteins. The N-terminal domain (N) of Trigger Factor mediates ribosome binding, whereas the middle domain (P) harbors peptidyl-prolyl isomerase activity. The function of the C-terminal domain (C) has remained enigmatic due to structural instability in isolation. Here, we have characterized a stabilized version ...

UNLABELLED Hepatitis B virus (HBV) DNA replication occurs within the HBV icosahedral core particles. HBV core protein (HBc) contains an arginine-rich domain (ARD) at its carboxyl terminus. This ARD domain of HBc 149-183 is known to be important for viral replication but not known to have a structure. Recently, nucleocapsid proteins of several viruses have been shown to contain nucleic acid chap...

Molecular chaperones (heat shock proteins) are important components of cellular networks, such as protein-protein and gene regulatory networks. Chaperones participate in the folding of immunologically important proteins, presentation of antigens and activation of the immune system. Here, we propose that chaperone-related immune dysfunction might be more general than was previously thought. Muta...

α-Crystallin can function as a molecular chaperone by preventing unwanted interactions. This paper presents the effects of aging and cataract on the chaperone-like properties of α-crystallin from soluble fractions from the cortex and nucleus of human lenses by using three assays : enzyme inactivation and two turbidity experiments. The three methods complemented each other. There was no decrease...

The histidine brace (His-brace) is a copper-binding motif that associated with both oxidative enzymes and proteinaceous copper chaperones. Here, we used biochemical structural methods to characterize mutants of His-brace-containing chaperone from Pseudomonas fluorescens (PfCopC). A total 15 amino acid variants in primary second sphere residues were produced characterised terms their redox prope...