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Raghavan Varadarajan

Raghavan Varadarajan

Indian Institute of Science
India

Overview

What is he best known for?

The fields of study he is best known for:

  • Gene
  • DNA
  • Amino acid

His primary areas of investigation include Crystallography, Protein structure, Stereochemistry, Biochemistry and Mutant. In the field of Crystallography, his study on Crystal structure overlaps with subjects such as Hydrolase. Raghavan Varadarajan combines subjects such as Sphere packing, Biological system, Molecule, Hydrogen bond and Small molecule with his study of Protein structure.

The Protein sequencing and Amino acid research he does as part of his general Biochemistry study is frequently linked to other disciplines of science, such as Thermostability, therefore creating a link between diverse domains of science. The Mutant study combines topics in areas such as Ectopic expression, Growth inhibition, Bacteria and Escherichia coli. His Binding site study deals with Mutation intersecting with Antibody, Immunogen, Virus and Virology.

His most cited work include:

  • Elucidation of factors responsible for enhanced thermal stability of proteins: a structural genomics based study. (215 citations)
  • Design of an HA2-based Escherichia coli expressed influenza immunogen that protects mice from pathogenic challenge (197 citations)
  • Residue depth: a novel parameter for the analysis of protein structure and stability (174 citations)

What are the main themes of his work throughout his whole career to date?

His scientific interests lie mostly in Crystallography, Biochemistry, Virology, Mutant and Protein structure. His Crystallography research integrates issues from Maltose-binding protein, Stereochemistry and Denaturation. His study looks at the relationship between Biochemistry and topics such as Biophysics, which overlap with Gp41.

His biological study spans a wide range of topics, including Epitope, Antibody and Immunogen. Raghavan Varadarajan usually deals with Epitope and limits it to topics linked to Binding site and Monoclonal antibody. In his study, which falls under the umbrella issue of Mutant, Plasmid maintenance is strongly linked to DNA gyrase.

He most often published in these fields:

  • Crystallography (33.33%)
  • Biochemistry (32.42%)
  • Virology (29.68%)

What were the highlights of his more recent work (between 2017-2021)?

  • Virology (29.68%)
  • Antibody (21.46%)
  • Epitope (23.74%)

In recent papers he was focusing on the following fields of study:

Raghavan Varadarajan mainly investigates Virology, Antibody, Epitope, Immunogenicity and Immunogen. His study on Virus is often connected to Protein engineering as part of broader study in Virology. His Epitope study combines topics in areas such as Mutant, Binding site and Deep sequencing.

His Binding site study improves the overall literature in Biochemistry. Raghavan Varadarajan studied Deep sequencing and Protein structure that intersect with Native state, Crystallography, Sequence analysis, Epistasis and Mutagenesis. His research integrates issues of Protein design, Neutralizing antibody and Glycoprotein in his study of Immunogen.

Between 2017 and 2021, his most popular works were:

  • HIV-1 vaccination by needle-free oral injection induces strong mucosal immunity and protects against SHIV challenge (25 citations)
  • Insights into protein structure, stability and function from saturation mutagenesis. (13 citations)
  • Insights into protein structure, stability and function from saturation mutagenesis. (13 citations)

In his most recent research, the most cited papers focused on:

  • Gene
  • DNA
  • Amino acid

The scientist’s investigation covers issues in Protein structure, Epitope, Computational biology, Mutant and Deep sequencing. His Protein structure study combines topics from a wide range of disciplines, such as Native state, Crystallography, Protein tertiary structure and Protein folding. Raghavan Varadarajan has included themes like Protein design, Immunogen and Binding site in his Epitope study.

His Binding site research is classified as research in Biochemistry. His work on Wild type as part of general Mutant study is frequently linked to Linker, therefore connecting diverse disciplines of science. In his research, Mutagenesis is intimately related to Epitope mapping, which falls under the overarching field of Deep sequencing.

This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.

Best Publications

Elucidation of factors responsible for enhanced thermal stability of proteins: a structural genomics based study.

Suvobrata Chakravarty;Raghavan Varadarajan.
Biochemistry (2002)

276 Citations

Design of an HA2-based Escherichia coli expressed influenza immunogen that protects mice from pathogenic challenge

Gayathri Bommakanti;Michael P Citron;Robert W Hepler;Cheryl Callahan.
Proceedings of the National Academy of Sciences of the United States of America (2010)

264 Citations

Elucidation of determinants of protein stability through genome sequence analysis.

Suvobrata Chakravarty;Raghavan Varadarajan;Raghavan Varadarajan.
FEBS Letters (2000)

216 Citations

Residue depth: a novel parameter for the analysis of protein structure and stability

Suvobrata Chakravarty;Raghavan Varadarajan.
Structure (1999)

213 Citations

Influenza hemagglutinin stem-fragment immunogen elicits broadly neutralizing antibodies and confers heterologous protection.

Vamsee V. A. Mallajosyula;Michael Citron;Francesca Ferrara;Xianghan Lu.
Proceedings of the National Academy of Sciences of the United States of America (2014)

174 Citations

Effects of buried ionizable amino acids on the reduction potential of recombinant myoglobin

Raghavan Varadarajan;Thomas E. Zewert;Harry B. Gray;Steven G. Boxer.
Science (1989)

166 Citations

Thermodynamics of protein-peptide interactions in the ribonuclease S system studied by titration calorimetry.

Patrick R. Connelly;Raghavan Varadarajan;Julian M. Sturtevant;Frederic M. Richards.
Biochemistry (1990)

165 Citations

Cloning, expression in Escherichia coli, and reconstitution of human myoglobin.

Raghavan Varadarajan;Alex Szabo;Steven G. Boxer.
Proceedings of the National Academy of Sciences of the United States of America (1985)

155 Citations

Refinement of the crystal structure of ribonuclease S. Comparison with and between the various ribonuclease A structures.

Eunice E. Kim;Raghavan Varadarajan;Harold W. Wyckoff;Frederic M. Richards.
Biochemistry (1994)

144 Citations

Depth: a web server to compute depth, cavity sizes, detect potential small-molecule ligand-binding cavities and predict the pKa of ionizable residues in proteins

Kuan Pern Tan;Thanh Binh Nguyen;Siddharth Patel;Raghavan Varadarajan.
Nucleic Acids Research (2013)

137 Citations

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