Statistics of crumpled paper.

A statistical study of crumpled paper is allowed by a minimal 1D model: a self-avoiding line bent at sharp angles--in which the elastic energy resides--put in a confining potential. Many independent equilibrium configurations are generated numerically and their properties are investigated. At small confinement, the distribution of segment lengths is log-normal in agreement with previous predictions and experiments.

Structural features of normal and mutant human lysosomal glycoside hydrolases deduced from bioinformatics analysis.

Lysosomal storage diseases are due to inherited deficiencies in various enzymes involved in basic metabolic processes. As with other genetic diseases, accurate structure data for these enzymatic proteins should help in better understanding the molecular effects of mutations identified in patients with the corresponding lysosomal diseases; however, no such three-dimensional (3D) structure data are available for many lysosomal enzymes. Thus, we herein intend to illustrate for an audience of molecular geneticists how structure information can nonetheless be obtained via a bioinformatics approach in the case of five human lysosomal glycoside hydrolases.

Evidence for a microglial reaction within the vestibular and cochlear nuclei following inner ear lesion in the rat.

Following unilateral inner ear lesion, astrocytes undergo hypertrophy in the deafferented vestibular and cochlear nuclei as shown by an increase in the level of glial fibrillary acid. The present study extends our understanding of vestibular and cochlear system plasticity by examining microglial changes in these deafferented nuclei. The microglial reaction was studied 1, 2, 4, 8, 14, 21, 28 and 42 days following the lesion with a monoclonal OX-42 antibody and lectins (Griffonia simplicifolia, B4 isolectin) labelled with horseradish peroxidase or fluorescein.

Redox mechanism for the chaperone activity of heat shock proteins HSPs 60, 70 and 90 as suggested by hydrophobic cluster analysis: hypothesis.

We have recently shown that the N-terminal ATPase fragment of hsp70 (1-375, composed of domains I and II) as well as the subsequent domain III (376-520) may share three-dimensional similarities with hsp60. In this study, we propose that domain III, common to the hsp60s and hsp70s is also found in the hsp90s and adopts a beta-alpha-beta Rossmann-folded structure which is encountered in the NAD-binding domain of dehydrogenases. Consequently, with the help of the domain IV (in hsp70s and hsp90s) or of hsp10/GroES (in hsp60s) and possibly that of auxilliary partners, the hsp molecules could act as "unfoldases" or "reset systems" by disrupting secondary structures through redox reactions on the main polypeptidic chain with which they interact.

Putative dimeric organization of nuclear receptor hormone-binding domains, deduced from hydrophobic cluster analysis.

2D hydrophobic cluster analysis (HCA) protein sequence processing, efficient at low levels of sequence identity, leads to a coherent scheme for the structural organization of the hormone-binding domains (HBDs) of nuclear receptors. The typical serine protease inhibitor (serpin) fold, previously proposed, is confirmed as a likely framework for the hormone-binding domain and leads to a logical dimerization. Furthermore, homo- or hetero-dimerization creates sites where hormone could likely be bound, itself being an active component of the dimerization.