Physics-based computational and theoretical approaches to intrinsically disordered proteins
Highlights•Liquid-liquid phase separation underlies the formation of membraneless
organelles within cells.•Theory and molecular simulations help to relate interactions at the …
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
Amyloid fibrils are β-sheet rich protein aggregates that are strongly associated with various
neurodegenerative diseases. Raman spectroscopy has been broadly utilized to investigate …
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 …
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 …
many chemical and biological phenomena in aqueous environments. This review focuses …
Heightened cold-denaturation of proteins at the ice–water interface
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 …
storage of biopharmaceuticals to cryo-EM analysis of protein complexes. The formation of an …
Temperature-dependent solvation modulates the dimensions of disordered proteins
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 …
sensitive to environmental conditions. We have used single-molecule Förster resonance …
The hydrophobic temperature dependence of amino acids directly calculated from protein structures
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 …
relative strength of this hydrophobic effect for each amino acid by mining a large set of …
The hydrophobic effect and its role in cold denaturation
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 …
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
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 …
the twin need for stability and the ability to change. Among all the solvents water plays the …
Reversible switching between two common protein folds in a designed system using only temperature
TL Solomon, Y He, N Sari, Y Chen… - Proceedings of the …, 2023 - National Acad Sciences
Naturally occurring metamorphic proteins have the ability to interconvert from one folded
state to another through either a limited set of mutations or by way of a change in the local …
state to another through either a limited set of mutations or by way of a change in the local …