Buscar
Mostrando ítems 1-10 de 16
Packing defects functionalize soluble proteins
(Wiley, 2015-03)
This work explores the participation of protein packing defects, the so-called dehydrons, in biochemical events. We delineate the enabling role of dehydrons as activators of nucleophilic groups. This activation results ...
Nanoscale electrostatic theory of epistructural fields at the water-protein interface
(American Institute of Physics, 2012-12)
Nanoscale solvent confinement at the protein-water interface promotes dipole orientations that are not aligned with the internal electrostatic field of a protein, yielding what we term epistructural polarization. To quantify ...
Breakdown of the Debye polarization ansatz at protein-water interfaces
(American Institute Of Physics, 2013-06)
The topographical and physico-chemical complexity of protein-water interfaces scales down to the sub-nanoscale range. At this level of confinement, we demonstrate that the dielectric structure of interfacial water entails ...
Adherence of Packing Defects in Soluble Proteins
(American Physical Society, 2003-07)
For protein structure to prevail in water, its backbone hydrogen bonds must be shielded from water attack, requiring a cluster of “wrapping” nonpolar groups. Thus, underwrapped regions are adhesive, as exogenous removal ...
Productive induced metastability in allosteric modulation of kinase function
(Wiley, 2014-07)
Allosteric modulators of kinase function are of considerable pharmacological interest as blockers or agonists of key cell-signaling pathways. They are gaining attention due to their purported higher selectivity and ...
Protein packing defects “heat up” interfacial water
(Springer, 2013-06-25)
Ligands must displace water molecules from their corresponding protein surface binding site during association. Thus, protein binding sites are expected to be surrounded by non-tightly-bound, easily removable water molecules. ...
Water promotes the sealing of nanoscale packing defects in folding proteins
(Iop Publishing, 2014-05)
A net dipole moment is shown to arise from a non-Debye component of water polarization created by nanoscale packing defects on the protein surface. Accordingly, the protein electrostatic field exerts a torque on the induced ...
The principle of minimal episteric distortion of the water matrix and its role in protein folding
(American Institute Of Physics, 2013-08)
A significant episteric (around a solid) distortion of the hydrogen-bond structure of water is promoted by solutes with nanoscale surface detail and physico-chemical complexity, such as soluble natural proteins. These ...
Drug leads for interactive protein targets with unknown structure
(Elsevier, 2016-04)
The disruption of protein?protein interfaces (PPIs) remains a challenge in drug discovery. The problem becomes daunting when the structure of the target protein is unknown and is even further complicated when the interface ...
Supramolecular evolution of protein organization
(Annual Reviews, 2013-12)
Abstract. Protein associations, whether transient or long-lasting, determine cellular processes and enable the cooperative and regulated functionalities characteristic of complex organisms. From a broad physical perspective, ...