Folding of beta-lactoglobulin analyzed by NMR

Development of Transgenic Mice Harboring Ovine Beta Lactoglobulin-Calcitonin Transgene

Principal component analysis of the pH-dependent conformational transitions of bovine beta-lactoglobulin monitored by heteronuclear NMR.

To clarify the pH-dependent conformational transitions of proteins, we propose an approach in which structural changes monitored by heteronuclear sequential quantum correlation (HSQC) spectroscopy were analyzed by using a principal component analysis (PCA). We use bovine beta-lactoglobulin, a protein widely used in protein folding studies, as a target. First, we measured HSQC spectra at various...

Millisecond protein folding studied by NMR spectroscopy.

Proteins are involved in virtually every biological process and in order to function, it is necessary for these polypeptide chains to fold into the unique, native conformation. This folding process can take place rapidly. NMR line shape analyses and transverse relaxation measurements allow protein folding studies on a microsecond-to-millisecond time scale. Together with an overview of current a...

pH-induced structural transitions in beta-lactoglobulin.

Pharmaceutique units/mg; Novo, Copenhagen, Denmark) and a-chymotrypsin (Choay, Paris, France) were, under appropriate conditions, added to the partially purified enzyme in final concentrations of 50 and 250 pg/ml and incubated at 37°C for different time intervals, ranging from 1 to 24 h. In all proteinase-treated preparations the DPP IV activity measured exceeded 90% of the original DPP IV acti...

NMR studies of protein folding

NMR spectroscopy is the method of choice for determining the structural details of unfolded and partially folded states of proteins. Here, the utility of NMR spectroscopy in characterizing such disordered states which populate protein folding pathways, is discussed. The relevance of the structural information obtained to protein folding mechanisms is examined critically. NMR spectroscopy can no...