Herbert Zuber mainly investigates Peptide sequence, Stereochemistry, Amino acid, Biochemistry and Phycoerythrocyanin. His Peptide sequence research integrates issues from Binding site and Bacteriochlorophyll. Herbert Zuber has included themes like Protein structure, Crystallography, Helix and Protein primary structure in his Stereochemistry study.
He interconnects Edman degradation and Mutant in the investigation of issues within Amino acid. His study in the fields of Chlamydomonas reinhardtii, Protein subunit and Methionine under the domain of Biochemistry overlaps with other disciplines such as Monellin. His Phycoerythrocyanin research is multidisciplinary, incorporating elements of Thermophile, Phycocyanobilin and Chromophore.
His main research concerns Biochemistry, Peptide sequence, Amino acid, Stereochemistry and Phycobiliprotein. Biochemistry and Bacteria are commonly linked in his work. The Protein primary structure research Herbert Zuber does as part of his general Peptide sequence study is frequently linked to other disciplines of science, such as Bilin, therefore creating a link between diverse domains of science.
His research in Amino acid intersects with topics in Residue, Nucleic acid sequence, Molecular biology and Rhodospirillum rubrum. His studies deal with areas such as Edman degradation, Molecular mass, Chromophore, Phycocyanobilin and Protein structure as well as Stereochemistry. The study incorporates disciplines such as Phycobilisome and Allophycocyanin in addition to Phycobiliprotein.
Herbert Zuber focuses on Biochemistry, Chlorosome, Circular dichroism, Amino acid and Biophysics. Herbert Zuber is investigating Circular dichroism as part of his Stereochemistry and Crystallography and Circular dichroism study. His research integrates issues of Isoleucine and Purple bacteria in his study of Stereochemistry.
His Amino acid study integrates concerns from other disciplines, such as Molecular biology, Binding protein, Nucleic acid sequence and Protein sequencing. Herbert Zuber combines subjects such as Phycobilisome and Allophycocyanin with his study of Biophysics. In the subject of general Peptide sequence, his work in Protein primary structure is often linked to Phycoerythrin, thereby combining diverse domains of study.
Herbert Zuber mainly focuses on Biochemistry, Amino acid, Allophycocyanin, Phycobilisome and Biophysics. Bacteriochlorophyll, Peptide sequence, Electrophoresis and Protein primary structure are among the areas of Biochemistry where Herbert Zuber concentrates his study. The concepts of his Amino acid study are interwoven with issues in Chlorosome, Sodium dodecyl sulfate, Open reading frame and Start codon.
His biological study spans a wide range of topics, including Cleavage, Edman degradation, Crystallography, Anabaena variabilis and Phycobiliprotein. Herbert Zuber has researched Phycobilisome in several fields, including Phycocyanin, Photochemistry and Sequence analysis. Negative stain, Linker, Trimer and Scanning transmission electron microscopy are fields of study that overlap with his Biophysics research.
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.
Thermal stability and protein structure.
Patrick Argos;Michael G. Rossmann;Ulrich M. Grau;Herbert Zuber.
X-ray crystallographic structure of the light-harvesting biliprotein C-phycocyanin from the thermophilic cyanobacterium Mastigocladus laminosus and its resemblance to globin structures
Tilman Schirmer;Wolfram Bode;Robert Huber;Walter Sidler.
Journal of Molecular Biology (1985)
Molecular structure of the bilin binding protein (BBP) from Pieris brassicae after refinement at 2.0 Å resolution
Robert Huber;Monika Schneider;Irmgard Mayr;Rudi Müller.
Journal of Molecular Biology (1987)
Refined three-dimensional structure of phycoerythrocyanin from the cyanobacterium Mastigocladus laminosus at 2.7 Å
Markus Duerring;Robert Huber;Wolfram Bode;Robert Ruembeli.
Journal of Molecular Biology (1990)
STRUCTURE AND FUNCTION OF LIGHT‐HARVESTING COMPLEXES AND THEIR POLYPEPTIDES
Photochemistry and Photobiology (1985)
Expression of the nuclear gene encoding oxygen-evolving enhancer protein 2 is required for high levels of photosynthetic oxygen evolution in Chlamydomonas reinhardtii.
Stephen P. Mayfield;Michele Rahire;Gerhard Frank;Herbert Zuber.
Proceedings of the National Academy of Sciences of the United States of America (1987)
The complete amino acid sequence of both subunits of C-phycocyanin from the cyanobacterium Mastigocladus laminosus.
Gerhard Frank;Walter Sidler;Herbert Widmer;Herbert Zuber.
Biological Chemistry (1978)
Characterization of chlorophyll a/b proteins of photosystem I from Chlamydomonas reinhardtii.
Roberto Bassi;Su Yin Bianca Maria Soen;Gerhard Frank;Herbert Zuber.
Journal of Biological Chemistry (1992)
The complete amino acid sequence of the bacteriochlorophyll c binding polypeptide from chlorosomes of the green photosynthetic bacterium Chloroflexus aurantiacus
Thomas Wechsler;Franz Suter;R.Clinton Fuller;Herbert Zuber.
FEBS Letters (1985)
The complete amino acid sequence of both subunits of allophycocyanin, a light harvesting protein-pigment complex from the cyanobacterium Mastigocladus laminosus.
Walter Sidler;Jürg Gysi;Erika Isker;Herbert Zuber.
Biological Chemistry (1981)
If you think any of the details on this page are incorrect, let us know.
We appreciate your kind effort to assist us to improve this page, it would be helpful providing us with as much detail as possible in the text box below: