Covalent Labeling with Diethylpyrocarbonate for Studying Protein Higher-Order Structure by Mass Spectrometry.

Characterizing a protein's higher-order structure is essential for understanding its function. Mass spectrometry (MS) has emerged as a powerful tool for this purpose, especially for protein systems that are difficult to study by traditional methods. To study a protein's structure by MS, specific chemical reactions are performed in solution that encode a protein's structural information into its mass.

Measuring the Energy Barrier of the Structural Change That Initiates Amyloid Formation.

Obtaining kinetic and thermodynamic information for protein amyloid formation can yield new insight into the mechanistic details of this biomedically important process. The kinetics of the structural change that initiates the amyloid pathway, however, has been challenging to access for any amyloid protein system. Here, using the protein β-2-microglobulin (β2m) as a model, we measure the kinetics and energy barrier associated with an initial amyloidogenic structural change.

Correction: The use of ion-selective membranes to study cation transport in hybrid organic-inorganic perovskites.

Correction for 'The use of ion-selective membranes to study cation transport in hybrid organic-inorganic perovskites' by Emily C. Smith et al., Phys.

The use of ion-selective membranes to study cation transport in hybrid organic-inorganic perovskites.

Using a methylammonium selective membrane in conjunction with electrochemical impedance spectroscopy, we measured ion migration in methylammonium lead triiodide (MAPbI) with a millisecond (ms) time constant under illumination. These values were consistent with the reported values of ionic conduction in thin-film perovskite solar cells. We monitored an electrochemical impedance response arising from ionic conductivity through MAPbI and a methylammonium selective layer.