Pinakpani Chakrabarti
Professor, Biochemistry

PhD: Indian Institute of Science, Bangalore, 1981

Research interest
 

Understanding the structure and folding of proteins and their interactions with other molecules, large and small, using biophysical techniques (especially, X-ray crystallography) and database analysis. Some specific topics are:

  • Identification of stabilizing interactions (like CH-p, CH-O, electrophile-nucleophile, aromatic-aromatic etc.) and their geometry
  • Analysis of protein conformation
  • Protein folding, threading and prediction of structures
  • Molecular modelling and dynamics
  • Molecular recognition, protein-protein complexation and ion-binding by proteins
  • Crystallography of proteins from phage lambda
  • Molecular design and docking
  • Bioinformatics and proteomics
  • Crystal packing and supramolecular assembly

Name of group members

Name

Period of stay

Working for/as

Presently at

Shrihari Sonavane

Sept, 2004 – present

PhD

 

Arumay Pal

Sept, 2003 – present

PhD

 

Mainak Guharoy

Sept, 2003 – present

PhD

 

Sumit Biswas

Aug, 2002 – present

PhD

 

Bhaskar Dasgupta

Oct, 2001 – present

PhD

 

Rudra Prasad Saha

July, 2001 – present

PhD

 

Rajasri Bhattacharyya Dec, 1999 – present PhD/RA  
Ranjit Prasad Bahadur Aug, 2000 – August, 2005 PhD Université Paris-Sud

Saptarshi Mandal

Sept, 2003 – June, 2004

PA

Anshin Software Pvt. Ltd., Kolkata

Tarun K. Mandal

Aug, 2003 – July, 2004

PA

Haldia Inst Tech

Ajit B. Datta

Aug, 1997 – Nov, 2004

PhD

Cornell Univ

Lipika Pal-Ray

Aug, 2002 – April, 2005

RA

Univ Albany

Debnath Pal

Aug, 1995 – Oct, 2000

PhD

Indian Institute Science

Uttamkumar Samanta

July, 1994 – Mar, 2001

PhD/RA

Univ Delaware


Important publications (ten)

  1. Guharoy M and Chakrabarti P (2005). Conservation and relative importance of residues across protein-protein interfaces. Proc. Natl. Acad. Sci. USA, 102, in press.
  2. Datta AB, Panjikar S, Weiss MS, Chakrabarti P and Parrack P (2005). Structure of CII: implications for recognition of direct-repeat DNA by an unusual tetrameric organization. Proc. Natl. Acad. Sci. USA, 102, 11242-11247.
  3. Bahadur RP, Chakrabarti P, Rodier F and Janin J (2004). A dissection of specific and non-specific protein-protein interfaces. J. Mol. Biol. 336, 943-955.
  4. Bhattacharyya R and Chakrabarti P (2003). Stereospecific interactions of proline residues in protein structures and complexes. J. Mol. Biol. 331, 925-940.
  5. Pal L, Chakrabarti P and Basu G (2003). Sequence and structure patterns in proteins from an analysis of the shortest helices: implications for helix nucleation. J. Mol. Biol. 326, 273-291.
  6. Chakrabarti P and Pal D (2001). The interrelationships of side-chain and main-chain conformations in proteins. Prog. Biophys. Mol. Biol. 76, 1-102.
  7. Pal D and Chakrabarti P (1999). Cis peptide bonds in proteins: residues involved, their conformations, interactions and locations. J. Mol. Biol. 294, 271-288.
  8. Chakrabarti P and Chakrabarti S (1998). CHO hydrogen bond involving proline residues in -helices. J. Mol. Biol. 284, 867-873.
  9. Chakrabarti P and Samanta U (1995). CH/ interaction in the packing of the adenine ring in protein structures. J. Mol. Biol. 251, 9-14.
  10. Chakrabarti P (1993). Anion binding sites in protein structures. J. Mol. Biol. 234, 463-482.

To see the list of full publications, click here.

Contact


pinak@boseinst.ernet.in, pinak_chak@yahoo.co.in