|
 
Gateways:
>>Webmail
>>Intranet
>>Library
Bioinformatics Centre
A.J.C. Bose Centenary Building,
P-1/12, CIT Scheme - VII M,
Kolkata - 700 054, India
|
|
Dr. SHUBHRA GHOSH DASTIDAR
|
|
|
Area of Research:
Structural dynamics of biomolecules
The atoms and molecules in a cell are always jiggling, dancing and bumping into each other and occasionally carrying out a specific reaction or a process. This forms the lifeline of all organisms. Hence it is important to understand how exactly this is choreographed. The most sophisticated experimental technology is only just beginning to give us a glimpse of this intricate dance but at a very coarse level. Computer simulations of this dance are increasingly providing much needed atomistic details. The general interest of our group is to gain novel insight into biology from the computer simulations of such events. Such methods can be used to both understand the dances and what happens when things go wrong that lead to a disease such as cancer. Using those information one can start designing drugs in a rational manner. Right now the p53-pathway and Bcl2 family are two primary areas of focus, where both are promising areas of cancer therapeutics.
We work in a truly interdisciplinary manner and so students/postdocs coming from various disciplines e.g. Chemistry, Physics, Biology, Computer Science etc. can contribute to our laboratory with their own domain of expertise and can expand knowledge in other areas.
Ph.D. position available:
MSc in Chemistry and CSIR/UGC NET qualified candidates can send CV by email.
Key
Publications:
Chakraborti S, Chakravarty D, Gupta S, Chatterji BP, Dhar G, Poddar A, Panda D, Chakrabarti P, Dastidar SG(*) and Bhattacharyya B (*),Discrimination of Ligands with Different Flexibilities Resulting from the Plasticity of the Binding Site in Tubulin, Biochemistry (In Press)
Dastidar SG, Lane DP, Verma CS. Why is F19Ap53 unable to bind MDM2? Simulations suggest crack propagation modulates binding, Cell Cycle 2012; 11: 2239-47.
Brown CJ, Dastidar SG , S. T. Quah, A. Lim, B. Chia, C. S. Verma. C-Terminal Substitution of MDM2 Interacting Peptides Modulates Binding Affinity by Distinctive Mechanisms PLoS One 2011; 6, e24122
Fuentes G, Dastidar SG, Madhumalar A, Verma CS. Role of
protein flexibility in the Discovery of New Drugs (Review
Article), Drug Dev Res 2011, 71, 26
Dastidar SG (*), Raghunathan D, Nicholson J, Hupp TR, Lane DP,
Verma CS (*). Chemical States of the N-terminal “lid” of MDM2
regulate p53 binding. Cell Cycle 2011; 10: 82-89.
Dastidar SG, Madhumalar A, Fuentes G, Lane DP, Verma CS.
Forces mediating protein-protein interactions: a computational
study of p53 "approaching" MDM2. Theor Chem Acc 2010;
125: 621.
Brown CJ, Dastidar SG, See H, Comber DW, Ortiz-Lombardía M,
Verma CS, Lane DP. Rational Design and biophysical
characterization of Thioredoxin-based aptamers: Insights into
peptide grafting. J Mol Biol 2010; 235: 871.
Dastidar SG, Lane DP and Verma CS. Multiple conformation give
rise to similar binding affinities: Molecular simulation of
p53-MDM2. J Am Chem Soc 2008; 130: 13514
(showcased in “JACS-Select”)
| |
|
|
|
|
©
Bioinformatics Centre (BIC), Bose Institute, Kolkata 2011, Last updated on:
August 29, 2012 | |
| |
|
