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crsi2015-Brochure.pdf       crsi2015-list1 of posters.pdf         crsi2015-list2 of posters.pdf       crsi2015-list of accommodation.pdf       crsi2015-programme.pdf

DR. S.Aravamudhan: Poster P18: find in list1-----------Dr. S. Aravamudhan: Life Member-in Hotel Ambient Executive L12










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Click, to jump to IBS2015 presentation

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.



DR.S.Aravamudhan attended
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: http://nehuacin.tripod.com/rscfd177-posting.html

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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.



DOC01.pdf

CLICK HERE for Abstract submitted for consideration



DOC02.pdf

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DOC03.pdf

DOC04.pdf


DOC05.pdf
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DOC06.pdf

DOC07.pdf


DOC08.pdf
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DOC09.pdf

DOC10.pdf


DOC11.pdf
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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

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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The Video below is made by converting the PPT file using a ppt to video conversion software for which the quality of the output video was deliberately set to be LOWER for reasons of smaller video file size enabling a conducive streaming. The original powerpoint file is available at the Link below for display.
http://www.ugc-inno-nehu.com/ibs2015.ppt


Website for the IBS2015 event:   http://www.ugc-inno-nehu.com/ibs2015.html


Right Click on the video panel: In the prop-up menu look for 'zoom' option:
in the prop-down at ZOOM click on Full Screen to display the presentation in the full screen;
this can be reversed by exit full screen option
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