Low crowding agent concentration destabilizes against pressure unfolding
نویسندگان
چکیده
منابع مشابه
Pressure-induced protein-folding/unfolding kinetics.
We use an off-lattice minimalist model to describe the effects of pressure in slowing down the folding/unfolding kinetics of proteins when subjected to increasingly larger pressures. The potential energy function used to describe the interactions between beads in the model includes the effects of pressure on the pairwise interaction of hydrophobic groups in water. We show that pressure affects ...
متن کاملCavities determine the pressure unfolding of proteins.
It has been known for nearly 100 years that pressure unfolds proteins, yet the physical basis of this effect is not understood. Unfolding by pressure implies that the molar volume of the unfolded state of a protein is smaller than that of the folded state. This decrease in volume has been proposed to arise from differences between the density of bulk water and water associated with the protein,...
متن کاملMolecular-crowding effects on single-molecule RNA folding/unfolding thermodynamics and kinetics.
The effects of "molecular crowding" on elementary biochemical processes due to high solute concentrations are poorly understood and yet clearly essential to the folding of nucleic acids and proteins into correct, native structures. The present work presents, to our knowledge, first results on the single-molecule kinetics of solute molecular crowding, specifically focusing on GAAA tetraloop-rece...
متن کاملCrowding Factor In Evolutionary Multi-Agent System For Multiobjective Optimization
In this paper an implementation of an Evolutionary MultiAgent System (EMAS) for multiobjective optimization in the Pareto sense is presented. Some basic ideas of Pareto optimization is shown. Also the idea of putting EMAS into work on multiobjective optimization is described. In particular the parameter called the crowding factor is presented and discussed. It is explained, what is the crowding...
متن کاملCrowding effects on the mechanical stability and unfolding pathways of ubiquitin.
The interiors of cells are crowded, thus making it important to assess the effects of macromolecules on the folding of proteins. Using the self-organized polymer (SOP) model, which is a coarse-grained representation of polypeptide chains, we probe the mechanical stability of ubiquitin (Ub) monomers and trimers ((Ub)(3)) in the presence of monodisperse spherical crowding agents. Crowding increas...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biophysical Chemistry
سال: 2017
ISSN: 0301-4622
DOI: 10.1016/j.bpc.2017.04.013