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 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'.
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.
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.
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Atomic structure of the actin:DNase I complex.
Wolfgang Kabsch;Hans Georg Mannherz;Dietrich Suck;Emil F. Pai.
Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution : implications for the mechanism of GTP hydrolysis
Emil F. Pai;Ute Krengel;Gregory A. Petsko;Roger S. Goody.
The EMBO Journal (1990)
STRUCTURE OF THE GUANINE-NUCLEOTIDE-BINDING DOMAIN OF THE HA-RAS ONCOGENE PRODUCT P21 IN THE TRIPHOSPHATE CONFORMATION
Emil F. Pai;Wolfgang Kabsch;Ute Krengel;Kenneth C. Holmes.
Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion
C. Enroth;B.T. Eger;K. Okamoto;T. Nishino.
Proceedings of the National Academy of Sciences of the United States of America (2000)
Crystal structure of metarhodopsin II.
Hui Woog Choe;Yong Ju Kim;Jung Hee Park;Takefumi Morizumi;Takefumi Morizumi.
Time−resolved X−ray crystallographic study of the conformational change in Ha−ras p21 protein on GTP hydrolysis
Ilme Schlichting;Steven C. Almo;Gert Rapp;Keith Wilson.
THREE-DIMENSIONAL STRUCTURES OF H-RAS P21 MUTANTS - MOLECULAR BASIS FOR THEIR INABILITY TO FUNCTION AS SIGNAL SWITCH MOLECULES
Ute Krengel;Ilme Schlichting;Anna Scherer;Renate Schumann.
An Extremely Potent Inhibitor of Xanthine Oxidoreductase CRYSTAL STRUCTURE OF THE ENZYME-INHIBITOR COMPLEX AND MECHANISM OF INHIBITION
Ken Okamoto;Bryan T. Eger;Tomoko Nishino;Shiro Kondo.
Journal of Biological Chemistry (2003)
Substrate positions and induced-fit in crystalline adenylate kinase.
E.F. Pai;W. Sachsenheimer;R.H. Schirmer;G.E. Schulz.
Journal of Molecular Biology (1977)
The catalytic mechanism of glutathione reductase as derived from x-ray diffraction analyses of reaction intermediates.
Emil F. Pai;Georg E. Schulz.
Journal of Biological Chemistry (1983)
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