His main research concerns Stereochemistry, Crystallography, Protein structure, Biochemistry and Crystal structure. His research integrates issues of Peptide, Hydrogen bond, Multiple isomorphous replacement and Binding site in his study of Stereochemistry. His Crystallography research is multidisciplinary, incorporating perspectives in Hydrolase, Molecular model, DNA and Thermostability.
His Protein structure research is multidisciplinary, relying on both Glutathione S-transferase, Glutathione, Serine and Immunoglobulin superfamily. His research investigates the connection between Biochemistry and topics such as Cytochrome b that intersect with problems in Evolutionary biology, Sequence alignment, Horizontal gene transfer and Cytochrome c. His Crystal structure study combines topics from a wide range of disciplines, such as Ligand, Molecule and Resolution.
Robert Huber mostly deals with Stereochemistry, Biochemistry, Crystallography, Crystal structure and Protein structure. The study incorporates disciplines such as Active site, Molecule, Hydrogen bond, Multiple isomorphous replacement and Binding site in addition to Stereochemistry. His study involves Enzyme, Amino acid and Cystathionine beta synthase, a branch of Biochemistry.
Robert Huber studies Amylase which is a part of Enzyme. His study in Crystallography is interdisciplinary in nature, drawing from both X-ray crystallography and Molecular model.
Environmental resource management, Ecosystem services, Agriculture, Climate change and Populism are his primary areas of study. His biological study spans a wide range of topics, including Spatial planning, Process and Land use. Within one scientific family, Robert Huber focuses on topics pertaining to Stakeholder under Ecosystem services, and may sometimes address concerns connected to Sustainable management.
His work in Agriculture addresses issues such as Environmental economics, which are connected to fields such as Common Agricultural Policy and Single market. As a part of the same scientific study, he usually deals with the Climate change, concentrating on Land use, land-use change and forestry and frequently concerns with Ecosystem. His study on Populism also encompasses disciplines like
His primary areas of investigation include Environmental resource management, Ecosystem services, Climate change, Agriculture and Populism. The various areas that he examines in his Environmental resource management study include Policy network analysis, Process and Land use. The study incorporates disciplines such as Biodiversity and Stakeholder in addition to Ecosystem services.
His Climate change study deals with Land use, land-use change and forestry intersecting with Ecosystem. The Agriculture study combines topics in areas such as Environmental economics, Sustainability and Cultural landscape. His Populism study combines topics in areas such as Democracy and Ideology.
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.
Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution
Johann Deisenhofer;Otto Epp;Kunio Miki;Robert Huber.
Nature (1985)
Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins.
Huber R;Carrell Rw.
Biochemistry (1989)
The refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment.
W Bode;I Mayr;U Baumann;R Huber.
The EMBO Journal (1989)
Human α1-proteinase inhibitor: Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function
Hartmut Loebermann;Ryoji Tokuoka;Johann Deisenhofer;Robert Huber.
Journal of Molecular Biology (1984)
The structure of a complex of recombinant hirudin and human alpha-thrombin
Timothy J. Rydel;K. G. Ravichandran;A. Tulinsky;Wolfram Bode.
Science (1990)
The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex.
Peter Sondermann;Robert Huber;Vaughan Oosthuizen;Vaughan Oosthuizen;Uwe Jacob.
Nature (2000)
Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1.
Franz-Xaver Gomis-Rüth;Klaus Maskos;Michael Betz;Andreas Bergner.
Nature (1997)
Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 Å and 1.9 Å resolution
Markus Marquart;Johann Deisenhofer;Robert Huber;Walter Palm.
Journal of Molecular Biology (1980)
Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes.
I. Sinning;G. J. Kleywegt;S. W. Cowan;P. Reinemer.
Journal of Molecular Biology (1993)
The structures of HsIU and the ATP-dependent protease HsIU-HsIV.
Matthias Bochtler;Claudia Hartmann;Hyun Kyu Song;Gleb P. Bourenkov.
Nature (2000)
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