Cells are crowded, but proteins are almost always studied in dilute aqueous buffer. We
review the experimental evidence that crowding affects the equilibrium thermodynamics of …

Practically, IgG charge can contribute significantly to thermodynamic nonideality, and hence
to solubility and viscosity. Biologically, IgG charge isomers exhibit differences in clearance …

In-cell nuclear magnetic resonance (NMR) spectroscopy offers the possibility to study
proteins and other biomolecules at atomic resolution directly in cells. As such, it provides …

Electrochemiluminescence (ECL) is a powerful electroanalytical transduction technique in
biosensing and clinic immunodiagnostics, however its practical applications for point-of-care …

Protein–protein interactions are fundamental to biology yet are rarely studied under
physiologically relevant conditions where the concentration of macromolecules can exceed …

Protein crystals with their precise, periodic array of functional building blocks have potential
applications in biomaterials, sensing, and catalysis. This paper describes how a highly …

Complex formation between cationic cytochrome c and the water‐soluble, poly‐anionic p‐
phosphonatocalix [6] arene (pclx6) was investigated. A crystal structure (at 1.8 Å resolution) …

Separation and identification of different proteins is one of the most fundamental tasks in
biochemistry that is typically achieved by electrophoresis and Western blot techniques. Yet …

Understanding how the crowded and complex cellular milieu affects protein stability and
dynamics has only recently become possible by using techniques such as in-cell nuclear …

Although essential to numerous biotech applications, knowledge of molecular recognition by
arginine-rich motifs in live cells remains limited. 1H, 15N HSQC and 19F NMR …