@article { ISI:000259337100008,
	title = {Heteronuclear dipolar decoupling effects on multiple-quantum and satellite-transition magic-angle spinning NMR spectra},
	journal = {Magnetic Resonance in Chemistry},
	volume = {46},
	number = {10},
	year = {2008},
	month = {OCT},
	pages = {948-954},
	publisher = {JOHN WILEY \& SONS LTD},
	type = {Article},
	address = {THE ATRIUM, SOUTHERN GATE, CHICHESTER PO19 8SQ, W SUSSEX, ENGLAND},
	abstract = {<p>We here report on the influence of heteronuclear dipolar decoupling on the Al-27 3QMAS, 5QMAS, and the double-quantum filter-satellite-transition magic-angle spinning (DQF-STMAS) spectra of a strongly dipolar-coupled system, gibbsite. The requirements for heteronuclear dipolar decoupling increase with the order of coherence evolving in the indirect dimension of a two-dimensional (2D) experiment. The isotropic line width of the high-resolution 2D spectra, in samples like gibbsite, is composed of four parts: the distribution of isotropic shifts (delta(ISO), delta(QIS)), the homogeneous broadening related to the proton-proton flip-flop terms, the Al-27-Al-27 homonulcear dipolar couplings, and the H-1-Al-27 heteronuclear dipolar couplings. It is shown that, even in the case of gibbsite, where a strong proton-proton bath exists, the main resolution limiting factor in these experiments resides in the H-1-Al-27 dipolar interaction. Copyright (C) 2008 John Wiley \&amp; Sons, Ltd.</p>},
	keywords = {heteronuclear broadening, heteronuclear decoupling, homogeneous broadening, MQMAS, quadrupolar nuclei, Solid-state NMR, STMAS, TPPM},
	issn = {0749-1581},
	doi = {10.1002/mrc.2286},
	author = {Ganapathy, Subramanian and Delevoye, L. and Arnoureux, J. P. and Madhu, Perunthiruthy K.}
}
@article { ISI:000324309600011,
	title = {Basic structural motif and major biophysical properties of Amyloid-beta are encoded in the fragment 18-35},
	journal = {Chemical Physics},
	volume = {422},
	number = {SI},
	year = {2013},
	month = {AUG},
	pages = {80-87},
	publisher = {ELSEVIER SCIENCE BV},
	address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS},
	abstract = {<p>Aggregation and misfolding of the amyloid beta (A beta) peptide is thought to initiate Alzheimer{\textquoteright}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.</p>},
	keywords = {Alzheimer{\textquoteright}s disease, Fluorescence correlation spectroscopy, Protein aggregation, Solid-state NMR},
	issn = {0301-0104},
	doi = {10.1016/j.chemphys.2013.01.010},
	author = {Chandrakesan, Muralidharan and Sarkar, Bidyut and Mithu, Venus Singh and Rajiv M. Abhyankar and Bhowmik, Debanjan and Nag, Suman and Sahoo, Bankanidhi and Shah, Riddhi and Gurav, Sushma and Banerjee, Raja and Dandekar, Sucheta and Jose, Jaya C. and Sengupta, Neelanjana and Madhu, Perunthiruthy K. and Maiti, Sudipta}
}
