<?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%">Chandrakesan, Muralidharan</style></author><author><style face="normal" font="default" size="100%">Sarkar, Bidyut</style></author><author><style face="normal" font="default" size="100%">Mithu, Venus Singh</style></author><author><style face="normal" font="default" size="100%">Rajiv M. Abhyankar</style></author><author><style face="normal" font="default" size="100%">Bhowmik, Debanjan</style></author><author><style face="normal" font="default" size="100%">Nag, Suman</style></author><author><style face="normal" font="default" size="100%">Sahoo, Bankanidhi</style></author><author><style face="normal" font="default" size="100%">Shah, Riddhi</style></author><author><style face="normal" font="default" size="100%">Gurav, Sushma</style></author><author><style face="normal" font="default" size="100%">Banerjee, Raja</style></author><author><style face="normal" font="default" size="100%">Dandekar, Sucheta</style></author><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><author><style face="normal" font="default" size="100%">Madhu, Perunthiruthy K.</style></author><author><style face="normal" font="default" size="100%">Maiti, Sudipta</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Basic structural motif and major biophysical properties of Amyloid-beta are encoded in the fragment 18-35</style></title><secondary-title><style face="normal" font="default" size="100%">Chemical Physics</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Alzheimer's disease</style></keyword><keyword><style  face="normal" font="default" size="100%">Fluorescence correlation spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein aggregation</style></keyword><keyword><style  face="normal" font="default" size="100%">Solid-state NMR</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%">AUG</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">SI</style></number><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%">422</style></volume><pages><style face="normal" font="default" size="100%">80-87</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Aggregation and misfolding of the amyloid beta (A beta) peptide is thought to initiate Alzheimer's disease (AD). Here we study the role played by its central segment (A beta(18-35)) in determining these properties. A beta(18-35) has a solubility of 18 mu M. The soluble fraction consists mainly of small oligomers, which have mixed beta-sheet and random coil structures. The monomer is mostly a random coil with some residual compactness. Aggregated A beta(18-35) forms fibrils of width 3.0 +/- 0.7 nm, which is consistent with a hairpin shape. Each of these properties has a close similarity to A beta(40). Remarkably, solid state NMR indicates that the fibrils also retain the secondary structure and tertiary contacts of A beta(40). This is the shortest fragment of A beta reported so far which preserves its fibrillar architecture, including the hairpin turn, as well as its solution phase conformational properties. Residues 18-35 should therefore be a key target of AD therapeutics. (C) 2013 Published by Elsevier B. V.&lt;/p&gt;</style></abstract><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.028
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