His primary scientific interests are in Stereochemistry, Biochemistry, Binding site, Active site and Peptide sequence. The various areas that Richard A. Engh examines in his Stereochemistry study include Papain, Pterin, Aldehyde oxidase, Multiple isomorphous replacement and Peptide bond. Richard A. Engh carries out multidisciplinary research, doing studies in Biochemistry and Serine Proteinase Inhibitors.
His research integrates issues of Factor Xa Inhibitor, Salt bridge, Hydrogen bond and Pyrrolidine in his study of Binding site. Richard A. Engh has researched Active site in several fields, including Sequence alignment, Hydrolase and Matrix metalloproteinase, Batimastat, Matrix metalloproteinase inhibitor. The study incorporates disciplines such as Molecular recognition, Substrate Interaction, Substrate, Protein structure and Peptide in addition to Peptide sequence.
His primary areas of investigation include Biochemistry, Stereochemistry, Protein kinase A, Kinase and Binding site. His Stereochemistry research includes themes of Protein structure, Enzyme inhibitor, Hydrogen bond and Active site. His Protein structure research is multidisciplinary, incorporating elements of Peptide sequence and Peptide.
Richard A. Engh interconnects Protein kinase C and Mutant in the investigation of issues within Protein kinase A. His studies in Binding site integrate themes in fields like Crystallography and Protein kinase B. His Molecule research is multidisciplinary, relying on both Crystal structure and Molecular dynamics.
His main research concerns Kinase, Stereochemistry, Protein kinase A, Biochemistry and ABL. His Kinase research incorporates themes from Tyrosine, Mutant and Binding site. He studied Binding site and Ribose that intersect with Drug discovery.
He has included themes like Crystallography, Phase and Small molecule in his Stereochemistry study. In his study, which falls under the umbrella issue of Protein kinase A, Plasma protein binding and Protein structure is strongly linked to Transferase. His work in the fields of Biochemistry, such as Cyclin-dependent kinase 2 and Cyclin-dependent kinase complex, intersects with other areas such as Firefly luciferin and Luciferin.
His main research concerns Kinase, Protein kinase A, Stereochemistry, Biochemistry and Transferase. His work deals with themes such as Tyrosine, Arginine, Cysteine and Catalysis, which intersect with Kinase. His Protein kinase A research is multidisciplinary, incorporating perspectives in Protein kinase B, Molecular recognition, Ribose, Binding site and Drug discovery.
Many of his studies on Stereochemistry apply to Small molecule as well. His Cyclin-dependent kinase 2 and Cyclin-dependent kinase complex study, which is part of a larger body of work in Biochemistry, is frequently linked to Luciferin and Firefly luciferin, bridging the gap between disciplines. His Transferase research integrates issues from Bifunctional, Plasma protein binding, Protein subunit, Protein–protein interaction and Protein structure.
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Accurate Bond and Angle Parameters for X-ray Protein Structure Refinement
Richard A. Engh;Robert Huber.
Acta Crystallographica Section A (1991)
The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases.
W. Bode;R. Engh;D. Musil;U. Thiele.
The EMBO Journal (1988)
The refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity.
D. Musil;D. Zucic;D. Turk;R.A. Engh.
The EMBO Journal (1991)
Crystal Structure of the Xanthine Oxidase-Related Aldehyde Oxido-Reductase from D. gigas
Maria J. Romão;Margarida Archer;Isabel Moura;José J. G. Moura.
Phosphotransferase and substrate binding mechanism of the cAMP-dependent protein kinase catalytic subunit from porcine heart as deduced from the 2.0 A structure of the complex with Mn2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5-24).
D. Bossemeyer;R.A. Engh;V. Kinzel;H. Ponstingl.
The EMBO Journal (1993)
Chalcone derivatives antagonize interactions between the human oncoprotein MDM2 and p53.
Raphael Stoll;Christian Renner;Silke Hansen;Stefan Palme.
X-ray Structure of Active Site-inhibited Clotting Factor Xa IMPLICATIONS FOR DRUG DESIGN AND SUBSTRATE RECOGNITION
H Brandstetter;A Kühne;W Bode;R Huber.
Journal of Biological Chemistry (1996)
Crystal structure of a thermostable type B DNA polymerase from Thermococcus gorgonarius.
Karl-Peter Hopfner;Andreas Eichinger;Richard A. Engh;Frank Laue.
Proceedings of the National Academy of Sciences of the United States of America (1999)
Protein Kinase A in Complex with Rho-Kinase Inhibitors Y-27632, Fasudil, and H-1152P: Structural Basis of Selectivity
Christine Breitenlechner;Michael Gassel;Hiroyoshi Hidaka;Volker Kinzel.
Staurosporine-induced conformational changes of cAMP-dependent protein kinase catalytic subunit explain inhibitory potential
Lars Prade;Richard A Engh;Andreas Girod;Volker Kinzel.
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