The inhibition of fibril formation of lysozyme by sucrose and trehalose.

The two disaccharides, trehalose and sucrose, have been compared in many studies due to their structural similarity. Both possess the ability to stabilise and reduce aggregation of proteins. Trehalose has also been shown to inhibit the formation of highly structured protein aggregates called amyloid fibrils.

Documentation of pressure ulcers in medical records at an internal medicine ward in university hospital in western Sweden.

Objectives: Pressure ulcers cause suffering, prolong care periods, and increase mortality. The aim was to describe and analyze the documentation of pressure ulcers and focused on the medical records from an internal medicine ward in a university hospital in western Sweden.

Methods: A quantitative, retrospective review of medical records was conducted for all care events (n = 1,458) with descriptive statistics.

Protonation and hydrogen bonding of Ca2+ site residues in the E2P phosphoenzyme intermediate of sarcoplasmic reticulum Ca2+-ATPase studied by a combination of infrared spectroscopy and electrostatic calculations.

Protonation of the Ca(2+) ligands of the SR Ca(2+)-ATPase (SERCA1a) was studied by a combination of rapid scan FTIR spectroscopy and electrostatic calculations. With FTIR spectroscopy, we investigated the pH dependence of C=O bands of the Ca(2+)-free phosphoenzyme (E2P) and obtained direct experimental evidence for the protonation of carboxyl groups upon Ca(2+) release. At least three of the infrared signals from protonated carboxyl groups of E2P are pH dependent with pK(a) values near 8.

FTIR studies on the bond properties of the aspartyl phosphate moiety of the Ca2+ -ATPase.

As part of our work to determine the bond properties of the aspartyl phosphate moiety of the Ca(2+)-ATPase (SERCA1a) phosphoenzymes, we analyzed Morse potentials of the bridging P-O bond as well as C=O bond strengths for the model compound acetyl phosphate and the two phosphoenzyme intermediates Ca(2)E1P and E2P. Reaction-induced infrared difference spectroscopy was used and a carbonyl band of E2P at 1708 cm(-1) in the presence of mM Mg(2+) was tentatively assigned to the carbonyl group of phosphorylated Asp(351) because of its sensitivity to divalent cations. This band is found at 1716 cm(-1) with mM Ca(2+), for Ca(2)E1P at 1717 cm(-1) with Mg(2+), and at 1719 cm(-1) with Ca(2+) and at 1718 cm(-1) for acetyl phosphate in the absence of divalent cations.