2016 - Fellow of the American Association for the Advancement of Science (AAAS)
1992 - Fellow of John Simon Guggenheim Memorial Foundation
Cytochrome b6f complex, Biochemistry, Cytochrome, Biophysics and Crystallography are his primary areas of study. His biological study spans a wide range of topics, including Thermophile, Cytochrome f, Stereochemistry and Plastoquinone. His Cytochrome research is multidisciplinary, incorporating elements of Protein structure, Q cycle and Hemeprotein, Heme.
William A. Cramer has researched Heme in several fields, including Photochemistry and Coenzyme Q – cytochrome c reductase. His Biophysics research includes elements of Colicin, Bacterial outer membrane and Inner membrane. His Crystallography study combines topics from a wide range of disciplines, such as Bilayer, Nuclear magnetic resonance spectroscopy, Organic chemistry, Lipid bilayer and Membrane protein.
William A. Cramer mainly investigates Cytochrome b6f complex, Colicin, Biochemistry, Cytochrome and Biophysics. His research integrates issues of Heme, Photochemistry, Stereochemistry, Cytochrome f and Plastoquinone in his study of Cytochrome b6f complex. His study in Colicin is interdisciplinary in nature, drawing from both Crystallography, Bacterial outer membrane, Membrane, Ion channel and Peptide.
His biological study spans a wide range of topics, including Protein structure and Lipid bilayer. His studies deal with areas such as Electron transport chain, Cytochrome c, Cytochrome C1, Coenzyme Q – cytochrome c reductase and Electron transfer as well as Cytochrome. The Biophysics study combines topics in areas such as Analytical chemistry, Chloroplast and Transmembrane protein.
The scientist’s investigation covers issues in Cytochrome b6f complex, Biophysics, Cytochrome, Biochemistry and Stereochemistry. His studies in Cytochrome b6f complex integrate themes in fields like Electron transport chain, Crystallography, Heme and Photochemistry, Electron transfer. His study in Biophysics is interdisciplinary in nature, drawing from both Photosynthetic reaction centre, Transmembrane protein, Bacterial outer membrane, Membrane and Chloroplast.
His research integrates issues of Reactive oxygen species, Cytochrome f, Photosystem I, Superoxide and Quinone in his study of Cytochrome. His work deals with themes such as Thylakoid, Protein subunit and Coenzyme Q – cytochrome c reductase, Stigmatellin, which intersect with Stereochemistry. His Colicin study integrates concerns from other disciplines, such as Drug export and Ion channel.
William A. Cramer focuses on Cytochrome b6f complex, Biophysics, Biochemistry, Cytochrome and Protein structure. The various areas that William A. Cramer examines in his Cytochrome b6f complex study include Coenzyme Q – cytochrome c reductase, Electrochemical gradient, Quinone binding, Heme and Cytochrome f. His Coenzyme Q – cytochrome c reductase research is multidisciplinary, incorporating perspectives in Semiquinone and Plastocyanin.
His work carried out in the field of Biophysics brings together such families of science as Crystallography, Bacterial outer membrane and Membrane protein. His work on Biochemistry is being expanded to include thematically relevant topics such as Botany. His Cytochrome research includes elements of Stereochemistry and Electron transfer.
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Structure of the Cytochrome b6f Complex of Oxygenic Photosynthesis: Tuning the Cavity
Genji Kurisu;Genji Kurisu;Huamin Zhang;Janet L. Smith;William A. Cramer.
Science (2003)
Sequence homology and structural similarity between cytochrome b of mitochondrial complex III and the chloroplast b6-f complex: position of the cytochrome b hemes in the membrane.
W R Widger;W A Cramer;R G Herrmann;A Trebst.
Proceedings of the National Academy of Sciences of the United States of America (1984)
Crystal structure of chloroplast cytochrome freveals a novel cytochrome fold and unexpected heme ligation
Sergio E Martinez;Deru Huang;Andrzej Szczepaniak;William A Cramer.
Structure (1994)
SOME NEW STRUCTURAL ASPECTS AND OLD CONTROVERSIES CONCERNING THE CYTOCHROME b6f COMPLEX OF OXYGENIC PHOTOSYNTHESIS.
W. A. Cramer;G. M. Soriano;M. Ponomarev;D. Huang.
Annual Review of Plant Physiology and Plant Molecular Biology (1996)
Structure-function of the channel-forming colicins.
W A Cramer;J B Heymann;S L Schendel;B N Deriy.
Annual Review of Biophysics and Biomolecular Structure (1995)
Full subunit coverage liquid chromatography electrospray ionization mass spectrometry (LCMS+) of an oligomeric membrane protein: cytochrome b(6)f complex from spinach and the cyanobacterium Mastigocladus laminosus.
Julian P. Whitelegge;Huamin Zhang;Rodrigo Aguilera;Ross M. Taylor.
Molecular & Cellular Proteomics (2002)
Nucleotide sequence of the gene for apocytochrome b‐559 on the spinach plastid chromosome: implications for the structure of the membrane protein
Reinhold G. Herrmann;Juliane Alt;Barbara Schiller;W.R. Widger.
FEBS Letters (1984)
Energy Transduction in Biological Membranes
William A. Cramer;David B. Knaff.
(1991)
Biological identity and diversity in photosynthesis and respiration: structure of the lumen-side domain of the chloroplast Rieske protein
Christopher J Carrell;Huamin Zhang;William A Cramer;Janet L Smith.
Structure (1997)
Transmembrane traffic in the cytochrome b6f complex.
William A. Cramer;Huamin Zhang;Jiusheng Yan;Genji Kurisu.
Annual Review of Biochemistry (2006)
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