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The purpose of this national symposium in chemistry is to provide a forum
for the scientists, teachers and students in the country to
participate and discuss the recent developments in chemical sciences.
All the sessions / lectures will be held in the conference hall of NIT-T
which will include invited lectures, short presentations and poster presentations.
<:::::::from the organizers as documented in:
Valedictory Video: From Dr. Karvembu, convener, crsimidyear2015, NIT, Trichy
Shuttle NMR Relaxometry
----An experimental Spectroscopic technique for concerns as expressed in the above presentation at 10th Midyear CRSI meeting:
The chemical and physical principles underlying protein function can only be unraveled by gaining insight into both structural and dynamic features. Relaxation measured at various lower field strengths and detected at high field with high spectral resolution provides dynamic information linked to structure. Relaxometry with a sample shuttle:
"Polarization at high field".
"Relaxation at a wide range of low fields:Detection at high field."
Electrostatics play an important role in many aspects of protein chemistry. However, the accurate determination of side chain proton affinity in proteins by experiment and theory remains challenging. In recent years the field of nuclear magnetic resonance spectroscopy has advanced the way that protonation states are measured, allowing researchers to examine electrostatic interactions at an unprecedented level of detail and accuracy. Experiments are now in place that follow pH-dependent 13C and 15N chemical shifts as spatially close as possible to the sites of protonation, allowing all titratable amino acid side chains to be probed sequence specifically. The strong and telling response of carefully selected reporter nuclei allows individual titration events to be monitored. At the same time, improved frameworks allow researchers to model multiple coupled protonation equilibria and to identify the underlying pH-dependent contributions to the chemical shifts.