Emil F. Pai

What is he best known for?

The fields of study he is best known for:

• Enzyme
• Gene
• Amino acid

Stereochemistry, Biochemistry, Protein structure, Crystallography and Enzyme are his primary areas of study. His Stereochemistry study integrates concerns from other disciplines, such as Oxidoreductase, Xanthine dehydrogenase, Substrate and Active site. His work on Amino acid, Binding protein and Nucleotide as part of general Biochemistry study is frequently linked to Histone octamer, therefore connecting diverse disciplines of science.

His Protein structure research includes elements of Lyase, Conformational change, Guanosine triphosphate and Effector. His Crystallography research includes themes of Laser and Binding site. The concepts of his Binding site study are interwoven with issues in Biophysics, Peptide sequence, Beta sheet, Skeletal muscle and Actin.

His most cited work include:

• Atomic structure of the actin:DNase I complex. (1552 citations)
• Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution : implications for the mechanism of GTP hydrolysis (910 citations)
• STRUCTURE OF THE GUANINE-NUCLEOTIDE-BINDING DOMAIN OF THE HA-RAS ONCOGENE PRODUCT P21 IN THE TRIPHOSPHATE CONFORMATION (740 citations)

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

His primary areas of study are Biochemistry, Stereochemistry, Crystallography, Enzyme and Crystal structure. His work on Protein structure, Xanthine dehydrogenase, Nucleotide and Mutant as part of general Biochemistry research is frequently linked to Glutathione reductase, thereby connecting diverse disciplines of science. His Xanthine dehydrogenase study incorporates themes from Oxidoreductase, Bovine milk, Cofactor and Xanthine.

The study incorporates disciplines such as Active site, Orotidine 5'-phosphate decarboxylase, Substrate, Dehydrogenase and Binding site in addition to Stereochemistry. His research integrates issues of Peptide sequence and Methanobacterium in his study of Binding site. The Crystallography study combines topics in areas such as X-ray crystallography, Crystallization, Synchrotron and GTP'.

He most often published in these fields:

• Biochemistry (49.54%)
• Stereochemistry (38.15%)
• Crystallography (24.31%)

What were the highlights of his more recent work (between 2013-2021)?

• Biochemistry (49.54%)
• Enzyme (22.77%)
• Stereochemistry (38.15%)

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

His primary scientific interests are in Biochemistry, Enzyme, Stereochemistry, Crystallography and Synchrotron. His study in Active site, Protein structure, Subfamily, Gene and NAD+ kinase is carried out as part of his Biochemistry studies. His research in Active site intersects with topics in Binding site and Trypanosoma.

His Enzyme research is multidisciplinary, incorporating perspectives in Cancer cell and Docking. His biological study spans a wide range of topics, including Xanthine Oxidoreductase, Trypanosoma brucei, Crystal structure, Dithiothreitol and Protomer. His Protein crystallization study in the realm of Crystallography connects with subjects such as Chip.

Between 2013 and 2021, his most popular works were:

• The role of dimer asymmetry and protomer dynamics in enzyme catalysis. (92 citations)
• Fixed target matrix for femtosecond time-resolved and in situ serial micro-crystallography. (82 citations)
• Fixed target matrix for femtosecond time-resolved and in situ serial micro-crystallography. (82 citations)

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

• Enzyme
• Gene
• Amino acid

Emil F. Pai mostly deals with Biophysics, Synchrotron, Biochemistry, Crystallography and Stereochemistry. His Biophysics research integrates issues from Hydrolase, Epitope, Paratope, Immunogen and Allosteric regulation. His Biochemistry and Enzyme, Dehydrogenase, Binding site, Protein structure and Small molecule investigations all form part of his Biochemistry research activities.

Emil F. Pai works in the field of Enzyme, focusing on Active site in particular. His study in Crystallography is interdisciplinary in nature, drawing from both Laser and Femtosecond. His Stereochemistry research is multidisciplinary, incorporating elements of Oxidoreductase, Xanthine oxidase, Xanthine dehydrogenase, Dithiothreitol and Oxidase test.