tag:blogger.com,1999:blog-53484793380760345702024-03-18T21:33:25.230-07:00M N PonnuswamyM.Sc.,Post M.Sc.,(Dip). Ph.D., D.Sc., FTNASc,Dr. M N Ponnuswamyhttp://www.blogger.com/profile/06984069049473954581noreply@blogger.comBlogger3125tag:blogger.com,1999:blog-5348479338076034570.post-46191665838114780242012-05-22T08:48:00.000-07:002012-05-22T08:48:02.302-07:00COMPUTATIONAL MOLECULAR BIOLOGY<div dir="ltr" style="text-align: left;" trbidi="on">
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<tr valign="top"><td align="center" bgcolor="#FFCC99" colspan="23" rowspan="1" valign="middle" width="507"><b><span style="color: #006600;"><span style="font-size: 18;">Investigations of Protein stability and Folding</span></span></b></td>
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The rate of expansion of information technology, its
associated use in depositing and accessing large number of biological
data has created unprecedented need for researchers and R&D
industry. Computational tools developed in conjunction with the wet-lab
techniques generate high levels of data as output. However these outputs
are massive and the computed biological information (bioinformatics)
provides us the ways and means to correlate these massive data with
knowledge. In this direction, our work addresses important problems in
molecular biology, like protein stability and folding. A series of
computational analyses were performed to elucidate the factors
responsible for it. Eventhough the experimental analyses of these
studies have provided a wealth of information, the computational
approaches has provided the key results to perform protein engineering
experiments. The most promising methods looking ahead are those that
systematically control false positive production rate by integrating
computation with information obtained from different experimental
angles. Further there is a place for computational analysis to augment
nascent experimental methods in evolving disciplines of functional
genomics and proteomics. <br /><br /> In line with this, a study
was carried out on single mutants of T4 and human lysozymes using free
energies and amino acid properties which demonstrate the importance of
classifying them based on secondary structure towards the stability.
Further the significance of secondary structural elements are identified
from the study of 1531 single mutants using hydrophobic profile,
long-range order, stabilization centers and amino acid conservation. In a
comparative analysis of thermophilic and its homologous mesophilic
proteins, we inferred the importance of hydrophobic free energy. We have
also analysed the stability upon buried, partially buried and surface
mutations based on different secondary structural elements using various
amino acid properties, and also proposed a method to predict the
stability of protein mutants. In the analysis of folding rate of
two-state proteins, the significance of various free energies of the
non-covalent interactions, amino acid properties and topological
parameters are explored.</span></td>
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<td align="center" bgcolor="#FFCC99" colspan="24" rowspan="1" valign="middle" width="510"><b><span style="color: #006600;"><span style="font-size: 18;">Role of amino acid properties to determine backbone </span></span></b><i><span style="color: #006600;"><span style="font-size: 18;">tau</span></span></i><span style="color: #006600;"><span style="font-size: 18;">(N-Calpha-C')</span></span><b><span style="color: #006600;"><span style="font-size: 18;"> stretching angle in peptides and proteins</span></span></b></td>
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The analysis of the basic geometry of amino acid residues
of protein structures has demonstrated the invariability of all the bond
lengths and bond angles except for tau, the backbone N-Calpha-C' angle.
This angle can be widened or contracted significantly from the
tetrahedral geometry to accommodate various other strains in the
structure. In order to accurately determine the cause for this
deviation, a survey is made for the t angles using the peptide
structures and the ultrahigh resolution protein structures. The average
deviation of N-Calpha-C' angles from tetrahedral geometry for each amino
acid in all the categories were calculated and then correlated with
forty-eight physiochemical, energetic and conformational properties of
amino acids. Linear and multiple regression analysis were carried out
between the amino acid deviation and the 48 properties. This study
confirms the deviation of tau angles in both the peptide and protein
structures but similar forces do not influence them. The peptide
structures are influenced by physical properties whereas as expected the
conformational properties influence the protein structures. And it is
not any single property that dominates the deviation but the combination
of different factors contributes to the tau angle deviation.</span></td>
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<td align="center" bgcolor="#FFCC99" colspan="23" rowspan="1" valign="middle" width="509"><b><span style="color: #006600;"><span style="font-size: 18;">Study of weak interactions in a few heterocyclic structures</span></span></b></td>
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The hydrogen bonding nature of the halogen atom acceptors are
analyzed statistically and the geometrical characteristics of this weak
hydrogen bonded interactions are studied for the oxygen, nitrogen and
carbon atom donors. The hybridization states of the donor atoms and the
different coordination environment of the halogen acceptors were also
considered. The distance and the directionality characteristic that
dictates the hydrogen bonds are given importance. Oxygen and nitrogen
donors showed similar characteristics of a strong hydrogen bond whereas
carbon donors had weak nature. The hydrogen bonding nature of the carbon
donor with halogen acceptor was proved from this analysis but within a
hydrogen…acceptor distance cutoff of 2.7Å. Different hybridization state
of the donor atoms did not produce significant deviation in the
interacting nature but the various coordination environments did show
some deviation.</span></td>
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Non-covalent interactions involving heteroaromatic ring
systems play a major role in determining the function of many chemical
as well as biological molecules. Therefore, detailed quantitative
analyses of the p-interactions (X-H…pi and pi…pi) were carried out for
nitrogen containing p-systems (isoxazole, imidazole and indole
moieties). Statistical analysis of the geometrical properties for the
oxygen, nitrogen and carbon atom donors with the heterocyclic p-system
acceptors showed that carbon donors participate relatively in large
numbers for X-H…pi interactions and they adopt T-shaped geometry. The
pi…pi interaction analysis was categorized into three types based on the
involvement of the heterocyclic pi-systems with themselves, with any
other benzene ring present in that particular structure and their
influence on the formation of pi-interactions between benzene-benzene
rings found in that particular compound. The pi-systems in all the three
categories prefer to form offset stacking pi…pi interaction geometry.
The benzene rings which normally favour the formation of T-shaped
geometry is found to prefer offset stacking geometry which may be due to
the influence of the heteroatom. The pi-systems in these heterocyclic
structures behaves similar to the Phenylalanine - Phenylalanine
interactions in proteins and therefore this quantitative analysis can
serve as a guide for structural and biological studies.</span></td>
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<td align="center" bgcolor="#FFCC99" colspan="23" rowspan="1" valign="middle" width="509"><b><span style="color: #006600;"><span style="font-size: 18;">Average Assignment Method for Predicting the Stability of Protein Mutants</span></span></b></td>
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Prediction of protein stability upon amino acid
substitutions is an important problem in molecular biology and it will
be helpful for designing stable mutants. In this work, we have analyzed
the stability of protein mutants using three different data sets of
1791, 1396 and 2204 mutants, respectively for thermal stability (DTm),
free energy change due to thermal (DDG) and denaturant denaturations
(DDGH2O), obtained from ProTherm database. We have classified the
mutants into 380 possible substitutions and assigned the stability of
each mutant using the information obtained with similar type of
mutations. We observed that this assignment could distinguish the
stabilizing and destabilizing mutants to an accuracy of 70-80% at
different measures of stability. Further, we have classified the mutants
based on secondary structure and solvent accessibility and observed
that the classification significantly improved the accuracy of
prediction. The classification of mutants based on helix, strand and
coil distinguished the stabilizing/destabilizing mutants at an average
accuracy of 82% and the correlation is 0.56; information about the
location of residues at the interior, partially buried and surface of a
protein correctly identified the stabilizing/destabilizing residues at
an average accuracy of 81% and the correlation is 0.59. The nine
sub-classifications based on three secondary structures and solvent
accessibilities improved the accuracy of assigning
stabilizing/destabilizing mutants to an accuracy of 84-89% for the three
datasets. Further, the present method is able to predict the free
energy change (DDG) upon mutations within the deviation of 0.64kcal/mol.
We suggest that this method could be used for predicting the stability
of protein mutants.</span></td>
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</div>Dr. M N Ponnuswamyhttp://www.blogger.com/profile/06984069049473954581noreply@blogger.comtag:blogger.com,1999:blog-5348479338076034570.post-69481444806122171632011-05-25T01:46:00.000-07:002011-06-16T00:49:37.204-07:00countries visited<div dir="ltr" style="text-align: left;" trbidi="on"><h3 style="margin-left: .75in; mso-list: l0 level1 lfo1; mso-text-indent-alt: -.25in; tab-stops: list 45.0pt .75in; text-align: justify; text-indent: -.75in;"><span lang="EN-GB" style="font-family: "Times New Roman"; font-size: 12pt; font-style: normal; font-weight: normal;"><span style="font: 7pt "Times New Roman";"> </span>(i)<span style="font: 7pt "Times New Roman";"> </span></span><span lang="EN-GB" style="font-family: "Times New Roman"; font-size: 10pt; font-style: normal;">CANADA </span></h3><div class="MsoBodyText" style="margin-left: .75in; tab-stops: list .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.25in;"> NSERC Postdoctoral Fellow<span style="font-weight: normal;"> (Aug 1981 – June 1984) in the Department of <br />
Chemistry, University of British Columbia, Vancouver, BC, Canada. </span></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: list .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.25in;"><br />
</div><div class="MsoNormal" style="margin-left: .75in; mso-list: l0 level1 lfo1; mso-text-indent-alt: -.25in; tab-stops: list 45.0pt .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.75in;"><span lang="EN-GB"><span style="font: 7pt "Times New Roman";"> </span>(ii)<span style="font: 7pt "Times New Roman";"> </span></span><b><span lang="EN-GB" style="font-size: 10pt;">UNITED STATES OF AMERICA (USA)</span></b><b><span lang="EN-GB" style="font-family: "Arial Narrow"; font-size: 10pt;"></span></b></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: list .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.25in;"><b><span lang="EN-GB"> Robert A. Welch Foundation Postdoctoral Fellow</span></b><span lang="EN-GB"> (June 1984 – June 1986) in the Division of Biochemistry, Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch at Galveston, Texas, USA.</span></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: list .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.25in;"><br />
</div><div class="MsoNormal" style="margin-left: .75in; mso-list: l0 level1 lfo1; mso-text-indent-alt: -.25in; tab-stops: list 45.0pt .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.75in;"><span lang="EN-GB"><span style="font: 7pt "Times New Roman";"> </span>(iii)<span style="font: 7pt "Times New Roman";"> </span></span><b><span lang="EN-GB" style="font-size: 10pt;">UNITED STATES OF AMERICA (USA)</span></b><b><span lang="EN-GB" style="font-family: "Arial Narrow"; font-size: 10pt;"></span></b></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: list .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.25in;"><b><span lang="EN-GB"> Robert A. Welch Foundation Postdoctoral Fellow</span></b><span lang="EN-GB"> (May 1987 – Aug 1987) in the Division of Biochemistry, Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch at Galveston, Texas, USA.</span></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: list .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.25in;"><br />
</div><div class="MsoNormal" style="margin-left: .75in; mso-list: l0 level1 lfo1; mso-text-indent-alt: -.25in; tab-stops: list 45.0pt .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.75in;"><span lang="EN-GB"><span style="font: 7pt "Times New Roman";"> </span>(iv)<span style="font: 7pt "Times New Roman";"> </span></span><b><span lang="EN-GB" style="font-size: 10pt;">UNITED STATES OF AMERICA (USA)</span></b></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: list .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.25in;"><b><span lang="EN-GB"> Robert A. Welch Foundation Postdoctoral Fellow</span></b><span lang="EN-GB"> (May 1988 – Aug 1988) in the Division of Biochemistry, Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch at Galveston, Texas, USA. </span></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: list .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.25in;"><br />
</div><div class="MsoNormal" style="margin-left: .75in; mso-list: l0 level1 lfo1; mso-text-indent-alt: -.25in; tab-stops: list 45.0pt .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.75in;"><span lang="EN-GB"><span style="font: 7pt "Times New Roman";"> </span>(v)<span style="font: 7pt "Times New Roman";"> </span></span><b><span lang="EN-GB" style="font-size: 10pt;">EGYPT </span></b></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: list .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.25in;"><span lang="EN-GB"> Participated in the discussion meeting (Jan 16 – 25, 1993) of Fourth International School and Workshop on Computational Crystallography held at Aswan, Egypt.</span></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: list .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.25in;"><br />
</div><h3 style="margin-left: .75in; mso-list: l0 level1 lfo1; mso-text-indent-alt: -.25in; tab-stops: list 45.0pt .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.75in;"><span lang="EN-GB" style="font-family: "Times New Roman"; font-size: 12pt; font-style: normal; font-weight: normal;"><span style="font: 7pt "Times New Roman";"> </span>(vi)<span style="font: 7pt "Times New Roman";"> </span></span><span lang="EN-GB" style="font-family: "Times New Roman"; font-size: 10pt; font-style: normal;">POLAND </span></h3><div class="MsoNormal" style="margin-left: .75in; tab-stops: list .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.25in;"><span lang="EN-GB"> Participated in </span><span lang="EN-GB" style="font-size: 11pt;">t</span><span lang="EN-GB">he discussion meeting (May 18- 26, 1994) of the 2<sup>nd</sup> International School and Symposium on Synchrotron Radiation in Natural Sciences at Jaszowiec, Poland.</span></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: list .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.25in;"><br />
</div><h3 style="margin-left: .75in; mso-list: l0 level1 lfo1; mso-text-indent-alt: -.25in; tab-stops: list 45.0pt .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.75in;"><span lang="EN-GB" style="font-family: "Times New Roman"; font-size: 12pt; font-style: normal; font-weight: normal;"><span style="font: 7pt "Times New Roman";"> </span>(vii)<span style="font: 7pt "Times New Roman";"> </span></span><span lang="EN-GB" style="font-family: "Times New Roman"; font-size: 10pt; font-style: normal;">ITALY </span></h3><div class="MsoBodyText" style="margin-left: .75in; tab-stops: list .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.25in;"><span style="font-weight: normal;"> Presented a paper at the International School on Crystallography (May 27 – June 5, 1994) of Molecular Biology held at Ettore Majorana Centre, Erice – Sicily, Italy.</span></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: list .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.25in;"><br />
</div><h3 style="margin-left: .75in; mso-list: l0 level1 lfo1; mso-text-indent-alt: -.25in; tab-stops: list 45.0pt .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.75in;"><span lang="EN-GB" style="font-family: "Times New Roman"; font-size: 12pt; font-style: normal; font-weight: normal;"><span style="font: 7pt "Times New Roman";"> </span>(viii)<span style="font: 7pt "Times New Roman";"> </span></span><span lang="EN-GB" style="font-family: "Times New Roman"; font-size: 10pt; font-style: normal;">GERMANY </span></h3><div class="MsoNormal" style="margin-left: .75in; tab-stops: list .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.25in;"><b><span lang="EN-GB"> DBT Overseas Research Associateship</span></b><span lang="EN-GB"> (Mar 1996 – May 1996) to work in collaboration with Prof. Dr. Udo Heinemann at the Department of Kristallographie, Centrum fur Molekulare Medizin, Berlin-Buch, Germany.</span></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: list .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.25in;"><br />
</div><h3 style="margin-left: .75in; mso-list: l0 level1 lfo1; mso-text-indent-alt: -.25in; tab-stops: list 45.0pt .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.75in;"><span lang="EN-GB" style="font-family: "Times New Roman"; font-size: 12pt; font-style: normal; font-weight: normal;"><span style="font: 7pt "Times New Roman";"> </span>(ix)<span style="font: 7pt "Times New Roman";"> </span></span><span lang="EN-GB" style="font-family: "Times New Roman"; font-size: 10pt; font-style: normal;">MALAYSIA </span><span lang="EN-GB" style="font-family: "Arial Narrow"; font-size: 10pt; font-style: normal;"></span></h3><div class="MsoNormal" style="margin-left: .75in; tab-stops: list .75in left 63.0pt 1.0in; text-align: justify; text-indent: -.25in;"><b style="mso-bidi-font-weight: normal;"><span lang="EN-GB"> Invited speaker</span></b><span lang="EN-GB"> for Asian Crystallographic Association (AsCA’98) Seminar on Crystallography (Oct 13 –15, 1998) held at Universitat Kebangasan, Bangi, Malaysia. </span></div><div class="MsoNormal" style="tab-stops: 63.0pt 1.0in; text-align: justify;"><br />
</div><h3 style="margin-left: .75in; mso-list: l0 level1 lfo1; mso-text-indent-alt: -.25in; tab-stops: list 45.0pt left .75in; text-align: justify; text-indent: -.75in;"><span lang="EN-GB" style="font-family: "Times New Roman"; font-size: 12pt; font-style: normal; font-weight: normal;"><span style="font: 7pt "Times New Roman";"> </span>(x)<span style="font: 7pt "Times New Roman";"> </span></span><span lang="EN-GB" style="font-family: "Times New Roman"; font-size: 10pt; font-style: normal;">SINGAPORE</span></h3><div class="MsoNormal" style="margin-left: .75in; tab-stops: .75in; text-align: justify; text-indent: -.25in;"><span lang="EN-GB"> Participated in the discussion meeting in the Department of Chemical Engineering National University of Singapore during October1998.</span></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: .75in; text-indent: -.25in;"><br />
</div><h3 style="margin-left: .75in; mso-list: l0 level1 lfo1; mso-text-indent-alt: -.25in; tab-stops: list 45.0pt left .75in; text-align: justify; text-indent: -.75in;"><span lang="EN-GB" style="font-family: "Times New Roman"; font-size: 12pt; font-style: normal; font-weight: normal;"><span style="font: 7pt "Times New Roman";"> </span>(xi)<span style="font: 7pt "Times New Roman";"> </span></span><span lang="EN-GB" style="font-family: "Times New Roman"; font-size: 10pt; font-style: normal;">GERMANY </span></h3><div class="MsoNormal" style="margin-left: .75in; tab-stops: .75in; text-align: justify; text-indent: -.25in;"><b><span lang="EN-GB"> INSA Visiting Scientist</span></b><span lang="EN-GB"> (Dec 2000 – Mar 2001) to work in collaboration with Prof. Dr. Udo Heinemann at the Department of Kristallographie, Centre for Molecular Medicine, Berlin-Buch, Germany.</span></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: .75in; text-align: justify; text-indent: -.25in;"><br />
</div><div class="MsoNormal" style="margin-left: .75in; mso-list: l0 level1 lfo1; mso-text-indent-alt: -.25in; tab-stops: list 45.0pt left .75in; text-align: justify; text-indent: -.75in;"><span lang="EN-GB"><span style="font: 7pt "Times New Roman";"> </span>(xii)<span style="font: 7pt "Times New Roman";"> </span></span><b><span lang="EN-GB" style="font-size: 10pt;">UNITED STATES OF AMERICA (USA)</span></b></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: .75in; text-align: justify; text-indent: -.25in;"><b><span lang="EN-GB"> Visiting Scientist</span></b><span lang="EN-GB"> (June-Aug 2002) to work in the collaborative project with Dr. Swaminathan in the Structural Biology Department, Brookhaven National Laboratory, Upton, New York, USA.</span></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: .75in; text-align: justify; text-indent: -.25in;"><br />
</div><div class="MsoNormal" style="margin-left: .75in; mso-list: l0 level1 lfo1; mso-text-indent-alt: -.25in; tab-stops: list 45.0pt left .75in; text-align: justify; text-indent: -.75in;"><span lang="EN-GB"><span style="font: 7pt "Times New Roman";"> </span>(xiii)<span style="font: 7pt "Times New Roman";"> </span></span><b><span lang="EN-GB" style="font-size: 10pt;">GERMANY </span></b></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: .75in; text-align: justify; text-indent: -.25in;"><b><span lang="EN-GB"> DAAD Visiting Scientist</span></b><span lang="EN-GB"> ( May 2004 – July 2004) to work in collaboration with Prof. Dr. Udo Heinemann at the Department of Kristallographie, </span><span lang="EN-GB">Centre for Molecular Medicine</span><span lang="EN-GB">, Berlin-Buch, Germany. </span></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: .75in; text-align: justify; text-indent: -.25in;"><br />
</div><div class="MsoNormal" style="margin-left: .75in; mso-list: l0 level1 lfo1; mso-text-indent-alt: -.25in; tab-stops: list 45.0pt left .75in; text-align: justify; text-indent: -.75in;"><span lang="EN-GB"><span style="font: 7pt "Times New Roman";"> </span>(xiv)<span style="font: 7pt "Times New Roman";"> </span></span><b><span lang="EN-GB" style="font-size: 10pt;">GERMANY </span></b></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: .75in; text-align: justify; text-indent: -.25in;"><b><span lang="EN-GB"> INSA Visiting Scientist</span></b><span lang="EN-GB"> (April 2006 – June 2006) to work in collaboration with Prof. Dr. Udo Heinemann at the Department of Kristallographie, </span><span lang="EN-GB">Centre for Molecular Medicine</span><span lang="EN-GB">, Berlin-Buch, Germany </span></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: .75in; text-align: justify; text-indent: -.25in;"><br />
</div><h3 style="margin-left: .75in; mso-list: l0 level1 lfo1; mso-text-indent-alt: -.25in; tab-stops: list 45.0pt left .75in; text-align: justify; text-indent: -.75in;"><span lang="EN-GB" style="font-family: "Times New Roman"; font-size: 12pt; font-style: normal; font-weight: normal;"><span style="font: 7pt "Times New Roman";"> </span>(xv)<span style="font: 7pt "Times New Roman";"> </span></span><span lang="EN-GB" style="font-family: "Times New Roman"; font-size: 10pt; font-style: normal;">JAPAN</span></h3><div class="MsoNormal" style="margin-left: .75in; tab-stops: .75in; text-align: justify; text-indent: -.25in;"><b style="mso-bidi-font-weight: normal;"><span lang="EN-GB"> Visiting Scientist</span></b><span lang="EN-GB"> (March 12-26, 2007) to work in collaboration with Prof. Yokohama at RIKEN/SPring8 centre, Japan.</span></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: .75in; text-indent: -.25in;"><br />
</div><div class="MsoNormal" style="margin-left: .75in; mso-list: l0 level1 lfo1; mso-text-indent-alt: -.25in; tab-stops: list 45.0pt left .75in; text-indent: -.75in;"><span lang="EN-GB"><span style="font: 7pt "Times New Roman";"> </span>(xvi)<span style="font: 7pt "Times New Roman";"> </span></span><b><span lang="EN-GB" style="font-size: 10pt;">SINGAPORE</span></b></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: .75in; text-align: justify; text-indent: -.25in;"><b style="mso-bidi-font-weight: normal;"><span lang="EN-GB"> Invited visitor</span></b><span lang="EN-GB"> to the Structural Biology Department, NanYang Technological University, Singapore during March 2007.</span></div><div class="MsoNormal" style="margin-left: .75in; tab-stops: .75in; text-indent: -.25in;"><br />
</div><div class="MsoNormal" style="margin-left: .75in; mso-list: l0 level1 lfo1; mso-text-indent-alt: -.25in; tab-stops: list 45.0pt left .75in; text-align: justify; text-indent: -.75in;"><span lang="EN-GB"><span style="font: 7pt "Times New Roman";"> </span>(xvii)<span style="font: 7pt "Times New Roman";"> </span></span><b><span lang="EN-GB" style="font-size: 10pt;">GERMANY </span></b></div><b><span lang="EN-GB" style="font-family: "Times New Roman"; font-size: 12pt;"> INSA Visiting Scientist</span></b><span lang="EN-GB" style="font-family: "Times New Roman"; font-size: 12pt;"> (Jan 2009 - April 2009) to work in collaboration with Prof. Dr. Udo Heinemann at the Department of Kristallographie, </span><span lang="EN-GB" style="font-family: "Times New Roman"; font-size: 12pt;">Centre for Molecular Medicine</span><span lang="EN-GB" style="font-family: "Times New Roman"; font-size: 12pt;">, Berlin-Buch, Germany </span></div>Dr. M N Ponnuswamyhttp://www.blogger.com/profile/06984069049473954581noreply@blogger.comtag:blogger.com,1999:blog-5348479338076034570.post-59939037568878483802011-04-29T05:54:00.000-07:002011-04-29T05:54:09.502-07:00photo<div dir="ltr" style="text-align: left;" trbidi="on"><div class="separator" style="clear: both; text-align: center;"><a href="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjXMECsLG5xksz9vPH1EJvD9SUbF2cJqhg4WIpU8lYuGhVxrgDW8S5Sfxwqco7sq5AnUL7t-lWGFyJHqg27MnD0opHKN0A8LbkSahASySkOEkTWG-cfyX_DvIL4Sd5PJtyXjON1liUm/s1600/mnp+sir+photo.JPG" imageanchor="1" style="margin-left: 1em; margin-right: 1em;"><img border="0" height="320" src="https://blogger.googleusercontent.com/img/b/R29vZ2xl/AVvXsEjXMECsLG5xksz9vPH1EJvD9SUbF2cJqhg4WIpU8lYuGhVxrgDW8S5Sfxwqco7sq5AnUL7t-lWGFyJHqg27MnD0opHKN0A8LbkSahASySkOEkTWG-cfyX_DvIL4Sd5PJtyXjON1liUm/s320/mnp+sir+photo.JPG" width="248" /></a></div><br />
</div>Dr. M N Ponnuswamyhttp://www.blogger.com/profile/06984069049473954581noreply@blogger.com