Carlo P. M. van Mierlo

TL;DR: In this study, the heat induced fibrilar aggregation of the whey protein beta-lactoglobulin is investigated at low pH and at low ionic strength and results indicate that the fibrils formed have a periodic structure with a period of about 25 nm and a thickness of one or two protein monomers.

TL;DR: A synthetic peptide corresponding to the 15 N-terminal residues of bovine pancreatic trypsin inhibitor, with serine replacing the two cysteine residues, has been characterized by 1H-nuclear magnetic resonance spectroscopy, confirming the conclusion of a previous paper, that the (30-51) intermediate is partially folded, with the N- terminal segment disordered.

TL;DR: An analogue of the important folding intermediate of BPTI with only the disulphide bond between Cys30 and Cys51 has been characterized by 1H and 15N NMR techniques, finding that the N-terminal 15 residues are very flexible, and the (1H, 1H) NOESY data show that these residues have no NOE interactions with the remainder of the molecule.

TL;DR: The orientation, conformation, and local stability of bovine alpha-lactalbumin adsorbed on polystyrene nanospheres is characterized at the residue level by hydrogen/deuterium exchange and 2D NMR spectroscopy and appears to initiate the adsorption-induced unfolding of BLA.

TL;DR: In this article, the authors studied the conformational changes of bovine alpha-lactalbumin induced by adsorption on a hydrophobic interface and showed that the resulting partially denatured state resembles a molten globule state.