New horizons in the extraction of bioactive compounds using deep eutectic solvents: A review
With the rapid development of ionic liquid analogues, termed 'deep eutectic solvents'(DESs),
and their application in a wide range of chemical and biochemical processes in the past …
and their application in a wide range of chemical and biochemical processes in the past …
[HTML][HTML] A practical guide to small angle X-ray scattering (SAXS) of flexible and intrinsically disordered proteins
AG Kikhney, DI Svergun - FEBS letters, 2015 - Elsevier
Small-angle X-ray scattering (SAXS) is a biophysical method to study the overall shape and
structural transitions of biological macromolecules in solution. SAXS provides low resolution …
structural transitions of biological macromolecules in solution. SAXS provides low resolution …
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 …
Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding
The mechanism of denaturation of proteins by urea is explored by using all-atom
microseconds molecular dynamics simulations of hen lysozyme generated on BlueGene/L …
microseconds molecular dynamics simulations of hen lysozyme generated on BlueGene/L …
Structural analysis of intrinsically disordered proteins by small-angle X-ray scattering
P Bernado, DI Svergun - Molecular biosystems, 2012 - pubs.rsc.org
Small-angle scattering of X-rays (SAXS) is an established method to study the overall
structure and structural transitions of biological macromolecules in solution. For folded …
structure and structural transitions of biological macromolecules in solution. For folded …
Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group
WK Lim, J Rösgen… - Proceedings of the …, 2009 - National Acad Sciences
The mechanism by which urea and guanidinium destabilize protein structure is
controversial. We tested the possibility that these denaturants form hydrogen bonds with …
controversial. We tested the possibility that these denaturants form hydrogen bonds with …
Role of solvation effects in protein denaturation: from thermodynamics to single molecules and back
Protein stability often is studied in vitro through the use of urea and guanidinium chloride,
chemical cosolvents that disrupt protein native structure. Much controversy still surrounds …
chemical cosolvents that disrupt protein native structure. Much controversy still surrounds …
On the mechanism of SDS‐induced protein denaturation
AK Bhuyan - Biopolymers: Original Research on Biomolecules, 2010 - Wiley Online Library
To understand the mechanism of ionic detergent‐induced protein denaturation, this study
examines the action of sodium dodecyl sulfate on ferrocytochrome c conformation under …
examines the action of sodium dodecyl sulfate on ferrocytochrome c conformation under …
Urea's action on hydrophobic interactions
For more than a century, urea has been commonly used as an agent for denaturing proteins.
However, the mechanism behind its denaturing power is still not well understood. Here we …
However, the mechanism behind its denaturing power is still not well understood. Here we …
Equilibrium study of protein denaturation by urea
Though urea is commonly used to denature proteins, the molecular mechanism of its
denaturing ability is still a subject of considerable debate. Previous molecular dynamics …
denaturing ability is still a subject of considerable debate. Previous molecular dynamics …