<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Chatterjee, Prathit</style></author><author><style face="normal" font="default" size="100%">Sengupta, Neelanjana</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Effect of the A30P mutation on the structural dynamics of micelle-bound alpha synuclein released in water: a molecular dynamics study</style></title><secondary-title><style face="normal" font="default" size="100%">European Biophysics Journal With Biophysics Letters</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">A30P mutation</style></keyword><keyword><style  face="normal" font="default" size="100%">Alpha synuclein</style></keyword><keyword><style  face="normal" font="default" size="100%">Kink formation</style></keyword><keyword><style  face="normal" font="default" size="100%">molecular dynamics simulation</style></keyword><keyword><style  face="normal" font="default" size="100%">Structural persistence</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2012</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAY</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">5</style></number><publisher><style face="normal" font="default" size="100%">SPRINGER</style></publisher><pub-location><style face="normal" font="default" size="100%">233 SPRING ST, NEW YORK, NY 10013 USA</style></pub-location><volume><style face="normal" font="default" size="100%">41</style></volume><pages><style face="normal" font="default" size="100%">483-489</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Atomistic molecular dynamics simulation has been used to probe the effect of the A30P mutation on the structural dynamics of micelle-bound, helical alpha Synuclein when released in an aqueous environment. On the timescales simulated, the effect of the mutation on the secondary structure is restricted to local changes close to the mutation site in the N-terminal helical domain. The changes are transient, and all residues except Lys23 recover their initial structure. The local behavior due to the mutation gives rise to a global difference in the A30P mutant in the form of a permanent kink in the N-terminal helical domain.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">5</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.274
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Jose, Jaya C.</style></author><author><style face="normal" font="default" size="100%">Sengupta, Neelanjana</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Molecular dynamics simulation studies of the structural response of an isolated A beta(1-42) monomer localized in the vicinity of the hydrophilic TiO2 surface</style></title><secondary-title><style face="normal" font="default" size="100%">European Biophysics Journal</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amyloid beta</style></keyword><keyword><style  face="normal" font="default" size="100%">beta-Sheet propensity</style></keyword><keyword><style  face="normal" font="default" size="100%">molecular dynamics simulation</style></keyword><keyword><style  face="normal" font="default" size="100%">TiO2 rutile surface</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2013</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUN</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">6</style></number><publisher><style face="normal" font="default" size="100%">SPRINGER</style></publisher><pub-location><style face="normal" font="default" size="100%">233 SPRING ST, NEW YORK, NY 10013 USA</style></pub-location><volume><style face="normal" font="default" size="100%">42</style></volume><pages><style face="normal" font="default" size="100%">487-494</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;We have probed the effect of a model hydrophilic surface, rutile TiO2, on the full-length amyloid beta (A beta(1-42)) monomer using molecular dynamics simulations. The rutile surface brings about sharp changes in the peptide's intrinsic behavior in a distance-dependent manner. The intrinsic collapse of the peptide is disrupted, while the beta-sheet propensity is sharply enhanced with increased proximity to the surface. The results may have implications for A beta self-assembly and fibrillogenesis on hydrophilic surfaces and should be taken into consideration in the design of novel nanomaterials for perturbing amyloidogenic behavior.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">6</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.474
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Jana, Asis K.</style></author><author><style face="normal" font="default" size="100%">Sengupta, Neelanjana</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Surface induced collapse of A beta(1-42) with the F19A replacement following adsorption on a single walled carbon nanotube</style></title><secondary-title><style face="normal" font="default" size="100%">Biophysical Chemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Adsorption</style></keyword><keyword><style  face="normal" font="default" size="100%">Amyloid beta peptide</style></keyword><keyword><style  face="normal" font="default" size="100%">carbon nanotube</style></keyword><keyword><style  face="normal" font="default" size="100%">Lateral mobility</style></keyword><keyword><style  face="normal" font="default" size="100%">molecular dynamics simulation</style></keyword><keyword><style  face="normal" font="default" size="100%">Surface induced collapse</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2013</style></year><pub-dates><date><style  face="normal" font="default" size="100%">DEC</style></date></pub-dates></dates><publisher><style face="normal" font="default" size="100%">ELSEVIER SCIENCE BV</style></publisher><pub-location><style face="normal" font="default" size="100%">PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS</style></pub-location><volume><style face="normal" font="default" size="100%">184</style></volume><pages><style face="normal" font="default" size="100%">108-115</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Spontaneous adsorption of the A beta peptide on the surface of a single-walled carbon nanotube, resulting in the prevention of its intrinsic propensity to form collapsed states, could be a plausible means to hinder the peptide's initial nucleation and self-assembly. We report here the effects of sharply reducing both aromatic and hydrophobic character within the peptide's central hydrophobic core on its free and surface behavior. In such an altered peptide, complete surface adsorption is found to induce, rather than prevent, the adsorbed peptide's collapse. The weakened surface interactions of the central hydrophobic core allow its greater translational mobility on the surface, thereby facilitating interactions that lead to compaction. Both the adsorption and the subsequent collapse are accompanied by a loss of surface hydration in the modified peptide. We further find that such a two-step dewetting leads to hydration levels comparable to that obtained after compaction of the free peptide. These insights may be leveraged for designing molecular surfaces for disrupting intrinsic A beta behavior. (C) 2013 Elsevier B.V. All rights reserved.&lt;/p&gt;</style></abstract><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;2.319&lt;/p&gt;</style></custom4></record></records></xml>