Division of Structural Biology & Bioinformatics
Scientists:
Dr. Alok K. Datta (Head)
Prof.Siddhartha Roy (Required)
Dr. Subrata Adak
Dr. C. N. Mandal
Dr. Debasish Bhattacharyya (Required)
Dr. (Mrs.) Nanda Ghoshal (Required)
Dr Chitra Dutta (Required Photo)
Dr. M.C.Bagchi (Required)
Dr. Soumen Datta
Vision: Structure-function analysis of various biological macromolecules using
multi-pronged approaches from different angles involving modern biological,
chemical and physical technologies.
Objectives:

Characterisation of potentially prospective biological macromolecules and
other small molecules of therapeutic interest against various diseases, e.g.
leishmania, cholera, cancer, diabetes and for other anti-inflamatory,
anticonvulsant and immunomodulatory activities.

Studies on protein-protein and protein-nucleic acid interactions applying
modern sophisticated technologies like nuclear magnetic resonance (NMR),
mass-spectrometry
Quantitative structure activity relationship (QSAR) and 3D-QSAR.


Development of software for prediction, modification and analysis of
macromolecular structures and for elucidating their interactions with bioactive molecules.
SRF/JRF/Project Assistant
Name
Designation
E-mail ID
Banibrata Sen
Subhankar Dolai
SRF
JRF
Rajesh Kumar Yadav
JRF
banibrata_rs@iicb.res.in
subhankar_rs@iicb.res.i
n
biochemrajesh@yahoo.
co.in
Swati Pal
JRF
Dr.Ruchira Mukherjee
Indrani Chowdhury
Srijata Mukherjee
Paromita Raha
Asit Kumar Manna
Subrata Debnath
Neeladri Sekhar Roy
Abhishek Mazumder
Anusri Bhattacharya
Mrs. Sujata Majumder
Mrs. Madhumita Patra
Ms. Gargi Maity
Ms. Sangeeta Nath
Ms. Reema
Bhattacharya
Mr. Somnath Mandal
Ms. Debashree De
Ms. Nupur Sengupta
R.A
SRA
SRF
SRF
JRF
JRF
JRF
JRF
JRF
SRF
SRF
SRF/ICMR
SRF/CSIR
SRF/CSIR
ru_chira@yahoo.com
indrani_cm@yahoo.com
srijata_mukherjee@yahoo.co.in
rahap@rediffmail.com
mak_in2001@yahoo.co.in
debnath.Subrata@rediffmail.com
neeladri_sekhar@yahoo.co.in
SRF/CSIR
JRF
JRF/UGC
Somenath_rs@iicb.res.in
debashreeiicb@yahoo.co.in
sengutanupur@gmail.com
Ms. Savita Bhutoria
Mr. Nahren Manuel
Mr. Sandeep Chhabra
Ms. Pooja Sharma
Mr. R.S.K. Vijayan
Ipsita Chanda
Anirban Dutta
Mr. Sisir Nandi
Ms. Payel Ghosh
JRF (UGC)
JRF (CSIR)
JRF (CSIR)
JRF (CSIR)
SRF (CSIR)
S.R.F
J.R.F
JRF
JRF
Sabyasachi Das
Sanjib Chatterjee
Sandip Paul
Sumit K. Bag
anusri_b@rediffmail.com
sujata_dgp@yahoo.com
madhumita_ucst@yahoo.co.in
gmaiti@yahoo.com
sangeeta_rs@iicb.res.in
das_reema@yahoo.com
savita_rs@iicb.res.in
mailnahren@yahoo.com
Sandeep.rs@iicb.res.in
pooja_rs@iicb.res.in
vijayan_rs@iicb.res.in
ipsita_chanda@yahoo.co.in
webanirban@gmail.com
P.A
P.A
P.A
P.A
sabyadas@yahoo.co.in
c_sanjib1@rediffmail.com
websandip@gmail.com
sumitbag@yahoo.com
Name
Designation
E-mail ID
Samir Kumar Roy
T.O
Subhagata Ghosh
T.O
shuvagata@yahoo.com
Mrs. Aparna Laskar
Mr. P. Gangopadhyay
T.O
Tech Officer
aparna_iicb@yahoo.com
Staff Members:
Important Publications in the last 5 years
Dutta, M., Delhi, P., Sinha, K.M., Banerjee, R.K. and Datta, A.K. (2001) Lack of
abundance of cytoplasmic CsA-binding protein renders free-living Leishmania
donovani resistant to cyclosporinA. J. Biol. Chem 276, 19294-19300.
Chakraborty, A., Das, I., Datta, R, Sen, B., Bhattacharya, D., Mandal, C.N. and Datta,
A.K. (2002) A single-domain cyclophilin from Leishmania donovani reactivates
soluble aggregates of adenosine kinase by isomerase-independent chaperone function.
J. Biol. Chem 277, 47451-47460.
Chakraborty, A., Sen, B., Datta, R. and Datta, A.K. (2004) Isomerase-Independent
chaperone function of cyclophilin ensures aggregation prevention of adenosine kinase
both in vitro and under in vivo conditions. Biochemistry 43, 11862-11872.
Brahma, A. and Bhattacharyya, D. (2004) UDP-galactose 4-epimerase from
Kluveromyces fragilis: Evidence for independent mutarotase site. Eur. J. Biochem.
271, 58-68.
Nayar, S., Brahma, A., Barat, B. and Bhattacharyya, D. (2004) UDP-galactose 4epimerase from Kluveromyces fragilis: Analysis of its hysteretic behavior in catalysis.
Biochemistry 43, 10212-10223.
Brahma, A. and Bhattacharyya, D. (2004) UDP-galactose 4-epimerase from
Kluveromyces fragilis: Existence of subunit independent functional site. FEBS Lett.
577, 27-34.
Bagchi, M.C., Maity, B.C., and Bose, S (2004) QSAR of anti tuberculosis drugs of
INH type using graphical invariants. J.Mol.Struc : Theochem 679 , 179-186.
Roy S, Semsey S, Liu M, Gussin GN, Adhya S. (2004) GalR represses galP1 by
inhibiting the rate-determining open complex formation through RNA polymerase
contact: a GalR negative control mutant. J.Mol Biol. 344, 669-18.
Datta, R., Das, I., Sen, B., Chakraborty, A., Adak, S., Mandal, C.N. and Datta, A.K.
(2005) Mutational analysis of the active site residues crucial for catalytic activity of
adenosine kinase from Leishmania donovani. Biochem. J 387, 591-600
Maiti A, Roy S. (2005) Switching DNA-binding specificity by unnatural amino acid
substitution. Nucleic Acids Res. 33, 5896-903.
Guha S, Sahu K, Roy D, Mondal SK, Roy S, Bhattacharyya K.(2005) Slow solvation
dynamics at the active site of an enzyme:implications for catalysis. Biochemistry 44,
8940-7.
Roy S, Dimitriadis EK, Kar S, Geanacopoulos M, Lewis MS, Adhya S.(2005)
Gal repressor-operator-hu ternary complex ::pathway of repressosome formation.
Biochemistry 44, 5373-80.
Datta AB, Roy S, Parrack P.(2005) Role of C-terminal residues in oligomerisation
and stability of lambda CII : implications for lysius-lysogeny decision of the phage. J.
Mol Biol. 345, 315-24.
Adak S. and Datta, A.K.(2005) Leishmania major encodes an unusual peroxidase that
is a close homologue of plant ascorbate peroxidase: a novel role of the transmembrane
domain.Biochem J. 390, 465-74.
Sen, B., Chakraborty, A., Datta, R., Bhattacharyya, D. and Datta, A.K. (2006)
Reversal of ADP-mediated aggregation of adenosine kinase by cyclophilin leads to its
reactivation. Biochemistry 45, 263-271.
Das S, Paul S & Dutta C. “Evolutionary constraints on codon and amino acid
usage in two strains of human pathogenic actinobacteria Tropheryma whipplei.(2006)
J Mol Evol. 2006 62(5):645-58.
Das S, Paul S & Dutta C. “Synonymous codon usage in adenoviruses: influence
of mutation, selection and protein hydropathy.(2006)Virus Res.117(2):227-36
Chattopadhyay S, Sinha NK, Banerjee S, Roy D, Chattopadhyay D, Roy S. (2006)
Small cationic protein from a marine turtle has beta-defensin-like fold and
antibacterial and antiviral activity. Proteins. (In Press)