Suvobrata Chakravarty

Systematic analysis of the effect of multiple templates on the accuracy of comparative models of protein structure (2008)

Chakravarty, Suvobrata, Godbole, Sucheta, Zhang, Bing, Berger, Seth, Sanchez, Roberto

Abstract Background Although multiple templates are frequently used in comparative modeling, the effect of inclusion of additional template(s) on model accuracy (when compared to that of...

A Procedure for Detection and Quantitation of Cavity Volumes in Proteins (2002)

Chakravarty, Suvobrata, Bhinge, Akshay, Varadarajan, Raghavan

Accurate identification of cavities is important in the study of protein structure, stability, design, and ligand binding. Identification and quantitation of cavities is a nontrivial problem because...

Elucidation of Factors Responsible for Enhanced Thermal Stability of Proteins: A Structural Genomics Based Study (2002)

Chakravarty, Suvobrata, Varadarajan, Raghavan

Understanding the molecular basis for the enhanced stability of proteins from thermophiles has been hindered by a lack of structural data for homologous pairs of proteins from thermophiles and...

A procedure for detection and quantitation of cavity volumes in proteins. Application to measure the strength of the hydrophobic driving force in protein folding (2002)

Chakravarty, Suvobrata, Bhinge, Akshay, Varadarajan, Raghavan

Accurate identification of cavities is important in the study of protein structure, stability, design, and ligand binding. Identification and quantitation of cavities is a nontrivial problem because...

A Procedure for Detection and Quantitation of Cavity Volumes in Proteins (2002)

Chakravarty, Suvobrata, Bhinge, Akshay, Varadarajan, Raghavan

Accurate identification of cavities is important in the study of protein structure, stability, design, and ligand binding. Identification and quantitation of cavities is a nontrivial problem because...

A procedure for detection and quantitation of cavity volumes in proteins. Application to measure the strength of the hydrophobic driving force in protein folding (2002)

Chakravarty, Suvobrata, Bhinge, Akshay, Varadarajan, Raghavan

Accurate identification of cavities is important in the study of protein structure, stability, design, and ligand binding. Identification and quantitation of cavities is a nontrivial problem because...

Elucidation of Factors Responsible for Enhanced Thermal Stability of Proteins: A Structural Genomics Based Study (2002)

Chakravarty, Suvobrata, Varadarajan, Raghavan

Understanding the molecular basis for the enhanced stability of proteins from thermophiles has been hindered by a lack of structural data for homologous pairs of proteins from thermophiles and...

Protein stabilization through phage display (2000)

Chakravarty, Suvobrata, Mitra, Nivedita, Queitsch, Iris, Surolia, Avadhesha, Varadarajan, Raghavan, Dubel, Stefan

RNase S consists of two proteolytic fragments of RNase A, residues 1–20 (S20) and residues 21–124 (S pro). A 15-mer peptide (S15p) with high affinity for S pro was selected from a phage display...

Elucidation of determinants of protein stability through genome sequence analysis (2000)

Chakravarty, Suvobrata, Varadarajan, Raghavan

Sequences of putative soluble proteins from complete genomes of eight thermophiles and 12 mesophiles were analyzed to gain insight into determinants of protein thermostability. The predator algorithm...

Protein stabilization through phage display (2000)

Chakravarty, Suvobrata, Mitra, Nivedita, Queitsch, Iris, Surolia, Avadhesha, Varadarajan, Raghavan, Dubel, Stefan

RNase S consists of two proteolytic fragments of RNase A, residues 1–20 (S20) and residues 21–124 (S pro). A 15-mer peptide (S15p) with high affinity for S pro was selected from a phage display...

Elucidation of determinants of protein stability through genome sequence analysis (2000)

Chakravarty, Suvobrata, Varadarajan, Raghavan

Sequences of putative soluble proteins from complete genomes of eight thermophiles and 12 mesophiles were analyzed to gain insight into determinants of protein thermostability. The predator algorithm...

Residue depth: A novel parameter for the analysis of protein structure and stability (1999)

Chakravarty, Suvobrata, Varadarajan, Raghavan

Accessible surface area is a parameter that is widely used in analyses of protein structure and stability. Accessible surface area does not, however, distinguish between atoms just below the protein...

Residue depth: A novel parameter for the analysis of protein structure and stability (1999)

Chakravarty, Suvobrata, Varadarajan, Raghavan

Accessible surface area is a parameter that is widely used in analyses of protein structure and stability. Accessible surface area does not, however, distinguish between atoms just below the protein...

Accuracy of structure-derived properties in simple comparative models of protein structures

Chakravarty, Suvobrata, Wang, Lei, Sanchez, Roberto

The accuracy of comparative models of proteins is addressed here. A set of 12 732 single-template models of sequences of known high-resolution structures was built by an automated procedure....

Accuracy of structure-derived properties in simple comparative models of protein structures

Chakravarty, Suvobrata, Wang, Lei, Sanchez, Roberto

The accuracy of comparative models of proteins is addressed here. A set of 12 732 single-template models of sequences of known high-resolution structures was built by an automated procedure....