Abstract:

Lytic polysaccharide monooxygenases (LPMOs) are relatively recently discovered enzymes that catalyse the oxidation of polysaccharides, leading to chain cleavage.  LPMOs has transformed our understanding of biomass degradation, and—moreover—are now critical components in the enzymatic breakdown of biomass in the second generation bioethanol industry.¹  We and others have also recently shown that LPMOs are key virulence factors in major plant diseases.²

Abstract: Recent experimental measurements of the transition path time distributions of proteins moving from the folded to the unfolded state and vice versa, presented the theory with challenges. Analysis of the results suggested barrier heights that are much lower than the free energies of activation of the observed transitions, what are these barrier heights? Secondly, beyond the mere feat of following a protein as it folds or unfolds, is there anything really useful that we can actually learn from such experiments? These questions lead to a few insights.

Abstract:

Abstract: Metals are required for life, and microbes have evolved a number of small molecules to compete for, acquire, and utilize metals. Metal-binding compounds are important in a number of fields – these compounds can alter the growth of the microbial communities, enhance plant yields, control harmful pathogens, deliver metals in diseases of deficiencies, or can be used for bioremediation. Systematic methods for the discovery of metal-small molecule complexes from biological samples remain limited.