Potential and limits of a colloid approach to protein solutions

Abstract

We critically discuss the application of colloid science concepts to better understand protein solution properties in the entire concentration range.

Nonlinear Mechanics of Colloidal Gels: Creep, Fatigue, and Shear-Induced Yielding

“…Such spectacular properties, which make colloidal gels all the more versatile, are difficult to model and call for more refined approaches than simple coarse-graining, including complementary modeling based on polymer or macromolecular approaches. The limits of simple colloidal descriptions have been recently discussed in the case of globular proteins [Sarangapani et al, 2015, Stradner andSchurtenberger, 2020]. Similarly, disentangling the influence of colloid physics from the polymer or macromolecular aspects of the particle on the rupture properties of colloidal gels remains an open challenge and could be of great help to fine-tune the gel rupture behavior.…”

Towards molecular movies with X-ray photon correlation spectroscopy

“…Thus, experimental XPCS results can directly be compared to simulation results and help to benchmark properties and importance of, e.g., macromolecular crowding, patchy interactions, dynamic cluster formation. 23,25 2.1 X-ray speckle visibility spectroscopy -measure faster than the detector…”

“…Here, we give a perspective on future exciting science questions in connection to biological aqueous solutions that can be addressed with XPCS at the new X-ray sources. [21][22][23] Specifically, we discuss the importance of understanding biomolecular condensates on the nanoscale and the role of the heterogeneities of liquid and supercooled water in biological activity. Furthermore, we highlight the state of the art XPCS capabilities and provide practical considerations for designing XPCS experiments.…”

Crowding in the Eye Lens: Modeling the Multisubunit Protein β-Crystallin with a Colloidal Approach

“…In recent years, microscopic mechanisms were studied in more detail in model systems, outlining, e.g., the importance of self-association for resulting dynamical properties ( 7 , 8 ), the relevance of translational-rotational coupling ( 9 ), and the relevance of hydrodynamic interactions for a quantitative understanding of protein diffusion ( 10 , 11 , 12 ). In this context, the explanatory power of colloid model systems for short-range diffusion in concentrated protein solutions proved successful ( 13 , 14 ) for a large range of globular proteins, including myoglobin ( 15 ), hemoglobin ( 16 ), ferritin ( 17 ), lysozyme ( 18 , 19 ), crystallin proteins ( 20 , 21 ), bovine serum albumin ( 11 , 22 ), and antibodies ( 7 , 8 , 12 , 23 ). However, only a few of these studies attempted to link to macroscopic dynamical and thermodynamical properties such as compressibility, viscosity, and dynamical arrest.…”