<?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%">Bose, Tanaya</style></author><author><style face="normal" font="default" size="100%">Kumar, Vaijayanti A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Critical role of select peptides in the loop region of G-rich PNA in the preferred G-quadruplex topology and stability</style></title><secondary-title><style face="normal" font="default" size="100%">Tetrahedron</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">ESI-MS study</style></keyword><keyword><style  face="normal" font="default" size="100%">G-quadruplex</style></keyword><keyword><style  face="normal" font="default" size="100%">Peptide nucleic acid</style></keyword><keyword><style  face="normal" font="default" size="100%">topology</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2017</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%">73</style></volume><pages><style face="normal" font="default" size="100%">1534-1540</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;An uncharged PNA 15mer sequence formed unimolecular antiparallel G-quadruplex similar to that observed for DNA-TBA. Replacement of `tt' loop regions by peptides which induce helices or turns were found to have unpresidented effect on the quadruplex topology and stability. This study opens up a completely new strategy of utilizing G-quadruplex formation to display the array of functional groups in the three dimensional space thus creating a possibility of getting closer to the dream of designed peptides with three dimensional structures as observed in catalytic protein folds. (C) 2017 Elsevier Ltd. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">12</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.377</style></custom4></record></records></xml>