The folding and assembly of globular trimeric proteins

SIGLEAvailable from British Library Document Supply Centre- DSC:DX172644 / BLDSC - British Library Document Supply CentreGBUnited Kingdo

The folding and assembly of globular trimeric proteins

SIGLEAvailable from British Library Document Supply Centre- DSC:DX172644 / BLDSC - British Library Document Supply CentreGBUnited Kingdo

Molecular chaperones in protein folding: the art of avoiding sticky situations

Molecular chaperones are a class of proteins that interact with the non-native conformations of other proteins. The major role of chaperones of the Hsp70 and Hsp60 families is to prevent aggregation of newly synthesized polypeptides and then to mediate their folding to the native state. As a result of functional studies of these proteins, there has been a revision of the long-held view that protein folding in the cell is a spontaneous process

Experimental and theoretical analyses of the domain architecture of mammalian protein disulphide-isomerase

The high resolution structure of full-length protein disulphide-isomerase (PDI) has not been determined, but the polypeptide is generally assumed to comprise a series of consecutive domains. Models of its domain organisation have been proposed on the basis of various sequence-based criteria and, more recently, from structural studies on recombinant fragments corresponding to putative domains. We here describe direct studies of the domain architecture of full-length mammalian PDI based on limited proteolysis of the native enzyme. The results are consistent with an emerging model based on the existence of 4 consecutive domains each with the thioredoxin fold. The model was further tested by expressing recombinant fragments corresponding to alternative domain models and to truncated domains; the observed properties of these purified fragments supported the 4-domain model. A multiple alignment of many PDI-like sequences was generated to test whether domain boundaries could be predicted from any features of the alignment, such as sequence variability or hydrophilicity; neither of these parameters reliably predicted the domain boundaries determined by experiment