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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:>

Would be outof Shillong station in connection with this event from 14thJuly 2015 to 3rd August 2015.
Click on the hotlinks below to display the journey ticket details for the journey
Train-Guwahati-15thJuly-06:00hrs-to-New Delhi-31hrsJourney
Flight-Delhi-17th July-13:00hrs-to-Chennai

List of accepted Abstracts for the 10th Midyear 2015 CRSI National Symposium in Chemistry

---POSTER SITE---POSTER LAY OUT-for-"1m x 1m" measure of diplay board---

PP-21     S. Aravamudhan     Averaging spectra for time dependent molecular geometry     North Eastern Hill University, Shillong


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Inserted on 11th Aug 2015: Soon after the event the above photographs have been extracted from the Photo gallery at!gallery/c1ylu

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."

Click on this link below of Bruker BIOSPIN webpage to know more....:
The above is feature from BRUKER e news: Magnetic Resonance e-News - July 2015. Your roundup of the latest application and product news from the field of magnetic resonance

Contemporary NMR Studies of Protein Electrostatics
A topic related to the matter contained in Event-03:- Jump to EVENT 03
and in Event-07:-Jump to EVENT 07
Annual Review of Biophysics

Vol. 44: 53-75 (Volume publication date June 2015)
First published online as a Review in Advance on February 26, 2015
DOI: 10.1146/annurev-biophys-083012-130351
Mathias A.S. Hass1 and Frans A.A. Mulder2
1-Institute of Chemistry, Gorlaeus Laboratories, Leiden University, 2300 RA Leiden, The Netherlands
2-Department of Chemistry and Interdisciplinary Nanoscience Center (iNANO), Aarhus University, DK-8000 Aarhus C, Denmark; email:

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.