The Department of Chemical Sciences in TIFR has an active group in solid-state nuclear magnetic resonance spectroscopy. Nuclear magnetic resonance (NMR) of matter in solution state plays a significant role in structural and dynamics analysis. However, membrane proteins and fibril systems, which play a great role in many of the functions of human body, are not easily amenable to X-ray crystallography and solution-state NMR, as they do not yield high-quality crystals and are not easily soluble and there comes the importance of solid-state NMR. Besides, solid-state NMR has applications in zeolites, polymers, and catalysis.
The solid-state NMR group is engaged in research ranging from theory, development of methods, and applications to zeolites, catalysts, and amyloid fibrils. The theory side focuses on the development of expansion methods to solving time-dependent Schrodinger equation and the convergence of the series expansions. The methods part is on the development of radiofrequency pulse schemes for the manipulation of spins to achieve better resolution, sensitivity, and geometry information. The applications are in order to obtain structural and dynamics information of a variety of compounds in the solid state with the methods developed in the group and others in vogue.
The solid-state NMR group has access to two spectrometers in the National Facility for High-Field NMR, TIFR. They are 500 and 700 MHz spectrometers each equipped with state-of-the-art probes and other necessary accessories. The group has also access to all the standard biophysical laboratory items and other analytical methods to characterise materials.
The group has recently made significant contributions in the area of amyloid fibrils. These include understanding metal-ion binding sites, the influence of metal ions and certain biphenyl radicals on the fibrilisation pathways and their effect on toxicity, and the role of certain parts of the fibril system Aβ42 in forming the established structural motifs. More details may be found here.