This webpage posting was on 22nd Jan. 2015
crsi2015-Brochure.pdf crsi2015-list1 of posters.pdf crsi2015-list2 of posters.pdf crsi2015-list of accommodation.pdf crsi2015-programme.pdf |
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to JUMP to SHEETS 1,2 & 3 CLICK HERE to JUMP to SHEETS 4,5 & 6 CLICK HERE to JUMP to SHEETS 7,8 & 9 CLICK HERE to JUMP to SHEETS 10,11, & 12 |
The display materials (in Table below this index) are available as image files and PDF files. Click on the images for dispaly in actual size of the images The link for pdf appears below the images respectively in each cell of the Table.  |
The Faraday Discussion 177Royal Society of Chemistry, as delegate. Temporally and Spatially Resolved Molecular Science Indian Institute of Science, Department of I.P.C.-12th - 14th January 2015 Postings are at Link: https://nehuacin.tripod.com/rscfd177-posting.html  |
The display materials (in Table below) are available as image files and PDF files.
Click on the images for dispaly in actual size of the images
The link for pdf appears below the images respectively in each cell of the Table.
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DOC01.pdf |
CLICK HERE for Abstract submitted for consideration  DOC02.pdf CLICK HERE to JUMP to TOP of index |
 DOC03.pdf |
 DOC04.pdf |
 DOC05.pdf CLICK HERE to JUMP to TOP of index |
 DOC06.pdf |
 DOC07.pdf |
 DOC08.pdf CLICK HERE to JUMP to TOP of index |
 DOC09.pdf |
 DOC10.pdf |
 DOC11.pdf CLICK HERE to JUMP to TOP of index |
 DOC12.pdf |
The materials presented as above have been accepted for publication in "Journal Material Science and Engineering"
The reviewers report on the contents of the manuscript submitted: Referees Report
The Final version of the manuscript is at :JMSE20150330-paper-final
NOTE: The embeded feature may not implement the automatic timings. Hence Click when ever necessary and proceed with the viewing.
Contemporary NMR Studies of Protein Electrostatics
A topic related to the matter contained in list of events at http://www.ugc-inno-nehu.com/events-2015.html
: 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: fmulder@chem.au.d
ABSTRACT
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.
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http://www.ugc-inno-nehu.com/ibs2015.ppt
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