Beyond the Hofmeister series: Ion-specific effects on proteins and their biological functions
HI Okur, J Hladílková, KB Rembert, Y Cho… - The Journal of …, 2017 - ACS Publications
Ions differ in their ability to salt out proteins from solution as expressed in the lyotropic or
Hofmeister series of cations and anions. Since its first formulation in 1888, this series has …
Hofmeister series of cations and anions. Since its first formulation in 1888, this series has …
Proline mechanisms of stress survival
X Liang, L Zhang, SK Natarajan… - Antioxidants & redox …, 2013 - liebertpub.com
Significance: The imino acid proline is utilized by different organisms to offset cellular
imbalances caused by environmental stress. The wide use in nature of proline as a stress …
imbalances caused by environmental stress. The wide use in nature of proline as a stress …
When phased without water: biophysics of cellular desiccation, from biomolecules to condensates
The molecular machinery that enables life has evolved in water, yet many of the organisms
around us are able to survive even extreme desiccation. Especially remarkable are single …
around us are able to survive even extreme desiccation. Especially remarkable are single …
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 …
Therapeutic protein aggregation: mechanisms, design, and control
CJ Roberts - Trends in biotechnology, 2014 - cell.com
Although it is well known that proteins are only marginally stable in their folded states, it is
often less well appreciated that most proteins are inherently aggregation-prone in their …
often less well appreciated that most proteins are inherently aggregation-prone in their …
Cosolvent effects on protein stability
Proteins are marginally stable, and the folding/unfolding equilibrium of proteins in aqueous
solution can easily be altered by the addition of small organic molecules known as …
solution can easily be altered by the addition of small organic molecules known as …
Effect of trehalose on protein structure
Trehalose is a ubiquitous molecule that occurs in lower and higher life forms but not in
mammals. Till about 40 years ago, trehalose was visualized as a storage molecule, aiding …
mammals. Till about 40 years ago, trehalose was visualized as a storage molecule, aiding …
A molecular mechanism for osmolyte-induced protein stability
TO Street, DW Bolen, GD Rose - Proceedings of the …, 2006 - National Acad Sciences
Osmolytes are small organic compounds that affect protein stability and are ubiquitous in
living systems. In the equilibrium protein folding reaction, unfolded (U)⇌ native (N) …
living systems. In the equilibrium protein folding reaction, unfolded (U)⇌ native (N) …
Chemistry of Hofmeister anions and osmolytes
The study of the interactions of salts and osmolytes with macromolecules in aqueous
solution originated with experiments concerning protein precipitation more than 100 years …
solution originated with experiments concerning protein precipitation more than 100 years …
A review of methods available to estimate solvent-accessible surface areas of soluble proteins in the folded and unfolded states
Solvent accessible surface area (SASA) of proteins has always been considered as a
decisive factor in protein folding and stability studies. It is defined as the surface …
decisive factor in protein folding and stability studies. It is defined as the surface …