Suvobrata (Suvo) Chakravarty, PhD
Dr. Chakravarty's lab's long-term interest is in understanding how protein-protein interactions (PPIs) on the chromosomes ultimately regulate the expressions of genes. They currently focus on understanding how proteins interact with histones, the key components of chromatin. They utilize a structure-function approach to understand and probe these interaction mechanisms. They are also developing experimental and computations methods for the detection and characterization of PPIs.
Areas of expertise:
Recombinant protein biochemistry, biophysical chemistry, structural biology, bioinformatics and computational biology
Chakravarty S*, Essel F, Lin T & Zeigler S (2015) Histone peptide recognition by KDM5B-PHD1, a case study, Biochemistry 54: 5766-5780.
Chakravarty S*, Sheng Z, Iverson B, Moore B (2012). h6-type anion-p in Biomolecular Recognition. FEBS Lett. 586: 4180-6.
Chakravarty S, Lei Zeng & Ming-Ming Zhou (2009). Structure and Site-Specific Recognition of Histone H3 by the PHD Finger of Human Autoimmune Regulator. Structure 17, 670-679.
Chakravarty S, Wang L & Sanchez R (2005). Accuracy of Structure-derived properties in Simple Comparative models of Protein Sctructure. Nucleic Acid Research 33, 244-259.
Chakravarty S, & Sanchez R (2004). Systematic Analysis of Added-value in Simple Comparative models of Protein Sctructure. Structure 12, 1461-1470.
Chakravarty S & Varadarajan R (2002). Elucidation of factors responsible for enhanced thermal stability of proteins: a structural genomics based study. Biochemistry 41, 8152-8161.
Chakravarty S, Bhinge A & Varadarajan R (2002). A procedure for detection and quantitation of cavity volumes in proteins: application to measure the strength of the hydrophobic driving force in protein folding. J Biol Chem 277, 31345-53.
Chakravarty S, Mitra N, Queitsch I, Surolia A, Varadarajan R, Dubel S (2000). Protein stabilization through phage display. FEBS Lett. 476, 296-300.
Chakravarty S & Varadarajan R (2000). Elucidation of determinants of protein stability through genome sequence analysis. FEBS Lett. 470, 65-69.
Chakravarty S & Varadarajan R (1999). Residue depth: a novel parameter for the analysis of protein structure and stability. Structure Fold Des. 7, 723-732.
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