Charles A. Haynes

TL;DR: In this article, the authors take a fresh look at the driving force for protein adsorption by combining recent advances with key results from the past and conclude that four effects, namely structural rearrangements in the protein molecule, dehydration of (parts of) the sorbent surface, redistribution of charged groups in the interfacial layer, and protein surface polarity usually make the primary contributions to the overall adorption behavior.

TL;DR: It is demonstrated that a single, complex gene locus in Bacteroides ovatus confers XyG catabolism in this common colonic symbiont, and the metabolism of even highly abundant components of dietary fibre may be mediated by niche species.

TL;DR: In this paper, structural perturbations and thermodynamic-stability changes in two similar-sized globular proteins, hen egg-white lysozyme and bovine milk α-lactalbumin, upon physical adsorption to either microspheres of a negatively charged polystyrene (PS-) latex or a dispersion of variably charged hematite (α-Fe2O3) are determined from differential scanning microcalorimetry (micro-DSC), isothermal titration micro-imaging, and more conventional electrophoretic-

TL;DR: In this paper, the adsorption of both plasmid and chromosomal duplex DNA to silica was investigated with the aim of determining the dominant forces involved in the binding reaction.

TL;DR: The crystal structures of an EPEC intimin carboxy-terminal fragment alone and in complex with the EPEC Tir intimin-binding domain are described, giving insight into the molecular mechanisms of adhesion of A/E pathogens.