Physics-based computational and theoretical approaches to intrinsically disordered proteins

JE Shea, RB Best, J Mittal - Current opinion in structural biology, 2021 - Elsevier
Highlights•Liquid-liquid phase separation underlies the formation of membraneless
organelles within cells.•Theory and molecular simulations help to relate interactions at the …

Exploring the structure and formation mechanism of amyloid fibrils by Raman spectroscopy: a review

D Kurouski, RP Van Duyne, IK Lednev - Analyst, 2015 - pubs.rsc.org
Amyloid fibrils are β-sheet rich protein aggregates that are strongly associated with various
neurodegenerative diseases. Raman spectroscopy has been broadly utilized to investigate …

Temperature, hydrostatic pressure, and osmolyte effects on liquid–liquid phase separation in protein condensates: physical chemistry and biological implications

H Cinar, Z Fetahaj, S Cinar, RM Vernon… - … A European Journal, 2019 - Wiley Online Library
Liquid–liquid phase separation (LLPS) of proteins and other biomolecules play a critical role
in the organization of extracellular materials and membrane‐less compartmentalization of …

The hydrophobic effects: Our current understanding

Q Sun - Molecules, 2022 - mdpi.com
Hydrophobic interactions are involved in and believed to be the fundamental driving force of
many chemical and biological phenomena in aqueous environments. This review focuses …

Temperature-dependent solvation modulates the dimensions of disordered proteins

R Wuttke, H Hofmann, D Nettels… - Proceedings of the …, 2014 - National Acad Sciences
For disordered proteins, the dimensions of the chain are an important property that is
sensitive to environmental conditions. We have used single-molecule Förster resonance …

The hydrophobic temperature dependence of amino acids directly calculated from protein structures

E Van Dijk, A Hoogeveen, S Abeln - PLoS computational biology, 2015 - journals.plos.org
The hydrophobic effect is the main driving force in protein folding. One can estimate the
relative strength of this hydrophobic effect for each amino acid by mining a large set of …

Heightened cold-denaturation of proteins at the ice–water interface

A Arsiccio, J McCarty, R Pisano… - Journal of the American …, 2020 - ACS Publications
The process of freezing proteins is widely used in applications ranging from processing and
storage of biopharmaceuticals to cryo-EM analysis of protein complexes. The formation of an …

The hydrophobic effect and its role in cold denaturation

CL Dias, T Ala-Nissila, J Wong-Ekkabut, I Vattulainen… - Cryobiology, 2010 - Elsevier
The hydrophobic effect is considered the main driving force for protein folding and plays an
important role in the stability of those biomolecules. Cold denaturation, where the native …

From structure and dynamics to biomolecular functions: The ubiquitous role of solvent in biology

S Mondal, B Bagchi - Current Opinion in Structural Biology, 2022 - Elsevier
Biological activity requires a solvent that can provide a suitable environment, which satisfies
the twin need for stability and the ability to change. Among all the solvents water plays the …

Temperature effects on hydrophobic interactions: Implications for protein unfolding

Q Sun, Y Fu, W Wang - Chemical Physics, 2022 - Elsevier
According to our recent studies on hydrophobic interactions, this work is devoted to
investigate the temperature effects on hydrophobic interactions. Regarding to hydrophobic …