Polysaccharide elasticity governed by chair-boat transitions of the glucopyranose ring

Article Abstract:

Many biologically important polysaccharides have pyranose rings consisting of five carbon atoms and one oxygen atom. They response to stress by elastic deformation, although it is assumed that the pyranose ring structure is inelastic. The pyranose ring has been identified as the structural unit controlling elasticity, using single-molecule force measurements. It is suggested that the polysaccharide elasticity is due to the forced elongation of the ring structure and a change from chair to boat like conformation.

Ligand binding (Biochemistry), Polysaccharides

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Mechanical unfolding intermediates in titin modules

Article Abstract:

Single proteins were engineered to have multiple copies of single immunoglobulin domains of human cardiac titin, to avoid the problems linked to heterogeneity of the modular, naturally occurring titin. The molecules were elongated and an abrupt extension of each domain was found before the first unfolding event. Disruption of the hydrogen bonds by site-directed mutagenesis eliminated the unfolding intermediate.

Proteins, Elastin

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Probing the chemistry of thioredoxin catalysis with force

Article Abstract:

A study explains the chemistry and the catalytic mechanism of Escherichia coli thioredoxin (Trx). The results prove that the regulation of Trx activity largely depends on the substrate conformational changes.

Analysis, Nuclear magnetic resonance spectroscopy, X-ray crystallography, Spectra, Catalysis, Structure, Chemical properties, Thioredoxin

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