Her primary scientific interests are in Protein structure, Stereochemistry, Biochemistry, Active site and Crystallography. Her Protein structure research is multidisciplinary, relying on both Biophysics, Chromophore and Binding site. Her work carried out in the field of Stereochemistry brings together such families of science as Nucleic acid sequence, Sulfur, Dimer, Sulfite and Nitrite reductase.
Her Biochemistry research incorporates elements of Epitope and Function, Cell biology. Elizabeth D. Getzoff interconnects Covalent bond, Zinc, Superoxide dismutase and Superoxide in the investigation of issues within Active site. Her studies in Superoxide dismutase integrate themes in fields like Mutant and Exon.
Elizabeth D. Getzoff mainly investigates Stereochemistry, Biochemistry, Protein structure, Photochemistry and Crystallography. Her Stereochemistry study combines topics in areas such as Nitric oxide synthase, Active site, Heme, Dimer and Electron transfer. Her Active site study integrates concerns from other disciplines, such as Superoxide and Hydrogen peroxide.
Her Biochemistry research integrates issues from Epitope and Biophysics. Elizabeth D. Getzoff combines subjects such as Peptide sequence and Plasma protein binding with her study of Protein structure. She has included themes like Zinc and Mutant in her Superoxide dismutase study.
Her main research concerns Photolyase, Biophysics, Biochemistry, Stereochemistry and Photobiology. Her research in Photolyase intersects with topics in Pyrimidine dimer, Photochemistry and Flavin adenine dinucleotide. Her research integrates issues of Fourier transform infrared spectroscopy and Redox, Semiquinone in her study of Photochemistry.
Her work deals with themes such as Protein structure, Arabidopsis, Proton transport and Self-assembly, which intersect with Biophysics. Her studies link Superoxide dismutase with Protein structure. Her work in Stereochemistry covers topics such as Tryptophan which are related to areas like Circular dichroism, UVR8 and Dimer.
Elizabeth D. Getzoff spends much of her time researching Biochemistry, Biophysics, Protein structure, Cryptochrome and Flavoprotein. Elizabeth D. Getzoff regularly links together related areas like Nitric oxide in her Biochemistry studies. Her Biophysics study incorporates themes from Self-assembly and Arabidopsis.
She focuses mostly in the field of Protein structure, narrowing it down to topics relating to Dimer and, in certain cases, Crystallography. Her biological study spans a wide range of topics, including Flavin adenine dinucleotide, Electron transport chain, Flavin group, Electron transfer and Photolyase. Her work carried out in the field of Flavin adenine dinucleotide brings together such families of science as Binding domain and Conformational change, Stereochemistry.
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Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase
Han Xiang Deng;Afif Hentati;John A. Tainer;Zafar Iqbal.
Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase.
John A. Tainer;Elizabeth D. Getzoff;Karl M. Beem;Jane S. Richardson.
Journal of Molecular Biology (1980)
Structure and mechanism of copper, zinc superoxide dismutase
John A. Tainer;Elizabeth D. Getzoff;Elizabeth D. Getzoff;Jane S. Richardson;David C. Richardson.
Structure of nitric oxide synthase oxygenase dimer with pterin and substrate.
Brian R. Crane;Brian R. Crane;Andrew S. Arvai;Dipak K. Ghosh;Chaoqun Wu.
Electrostatic recognition between superoxide and copper, zinc superoxide dismutase
Elizabeth D. Getzoff;John A. Tainer;Paul K. Weiner;Peter A. Kollman.
Early abscisic acid signal transduction mechanisms: newly discovered components and newly emerging questions
Katharine E. Hubbard;Noriyuki Nishimura;Kenichi Hitomi;Elizabeth D. Getzoff.
Genes & Development (2010)
1.4 Å structure of photoactive yellow protein, a cytosolic photoreceptor: Unusual fold, active site, and chromophore
Gloria E. O. Borgstahl;DeWight R. Williams;Elizabeth D. Getzoff.
Structure of the fibre-forming protein pilin at 2.6 Å resolution
Hans E. Parge;Katrina T. Forest;Michael J. Hickey;Deborah A. Christensen.
The reactivity of anti-peptide antibodies is a function of the atomic mobility of sites in a protein.
John A. Tainer;Elizabeth D. Getzoff;Hannah Alexander;Richard A. Houghten.
Structural mechanism of abscisic acid binding and signaling by dimeric PYR1.
Noriyuki Nishimura;Kenichi Hitomi;Kenichi Hitomi;Andrew S. Arvai;Robert P. Rambo.
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