<?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%">Sarkar, Sujit</style></author><author><style face="normal" font="default" size="100%">Pandey, Prithvi Raj</style></author><author><style face="normal" font="default" size="100%">Roy, Sudip</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Propensity of self-assembled leucine-lysine diblock copolymeric alpha-helical peptides to remain in parallel and antiparallel alignments in water</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Physical Chemistry B</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2015</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUL</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">30</style></number><publisher><style face="normal" font="default" size="100%">AMER CHEMICAL SOC</style></publisher><pub-location><style face="normal" font="default" size="100%">1155 16TH ST, NW, WASHINGTON, DC 20036 USA</style></pub-location><volume><style face="normal" font="default" size="100%">119</style></volume><pages><style face="normal" font="default" size="100%">9520-9531</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Molecular dynamics Simulation study of alpha-helical diblock copolypeptides: preassembled in parallel and antiparallel alignments in water are presented. The assembled peptide lamellar structures were not disrupted even: after performing three step simulation protocols. Primarily hydrogen bonds between peptide are responsible for the stability: The analysis of the trajectory also suggests that Water plays a significant role in favoring self assembly We have detected continuous hydrogen bonded network structure, which is further responsible for the stability Of the lamellar structures. We have performed a detailed analysis of the hydrogen bonded network structure and its length. Further, free energy calculations revealed that the degree of stability for both lamellae are similar. The present study provides structural insight into the stability of self-assembled structures of block copolypeptides.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">30</style></issue><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%">3.187</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%">Sarkar, Sujit</style></author><author><style face="normal" font="default" size="100%">Chakraborty, Souvik</style></author><author><style face="normal" font="default" size="100%">Roy, Sudip</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Phase diagram of self-assembled sophorolipid morphologies from mesoscale simulations</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Molecular Liquids</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Bolaamphiphile</style></keyword><keyword><style  face="normal" font="default" size="100%">Flip frequency</style></keyword><keyword><style  face="normal" font="default" size="100%">Mesoscale simulation</style></keyword><keyword><style  face="normal" font="default" size="100%">Orientation of chains</style></keyword><keyword><style  face="normal" font="default" size="100%">Self-assembly</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2018</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAR </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">254</style></volume><pages><style face="normal" font="default" size="100%">198-207</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 constructed a phase diagram from the self-assembled morphologies of linolenic acid sophorolipid in water by performing mesoscale simulations in different concentrations. The dependence of morphologies and its properties of the self-assembled structure as a function of the concentration of bolaamphiphile in water are investigated. Two hydrophilic head groups and one hydrophobic tail group of bolaamphiphile have been mapped to beads for mesoscale simulation. The interaction parameters between different beads are calculated using Flory-Huggins solution theory. Flory-Huggins x-parameters have been calculated from atomistic simulation and experimental data of pure components constituting linolenic acid sophorolipid. We have obtained different self-assembled morphologies depending upon the concentrations of sophorolipid in water. We have explored the arrangements of hydrophobic and hydrophilic groups of the sophorolipid chains in the different morphologies. The sophorolipid chains found to be present in different structural arrangements. The residence time and flip frequency of these lipids in different orientations have been calculated and discussed in this work. (C) 2018 Elsevier B.V. All rights reserved.&lt;/p&gt;</style></abstract><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">3.648</style></custom4></record></records></xml>