Wayne A. Fenton focuses on Biochemistry, GroEL, Chaperonin, Protein folding and GroES. His study looks at the relationship between Biochemistry and fields such as Biophysics, as well as how they intersect with chemical problems. His Protein folding study combines topics in areas such as Thermosome and Foldase.
His research in Foldase focuses on subjects like GroES Protein, which are connected to GroEL Protein, Operon and Protein biosynthesis. He merges GroES with Opposite ring in his study. His studies in ATP hydrolysis integrate themes in fields like Folding and Binding site.
His primary scientific interests are in Biochemistry, GroEL, Chaperonin, GroES and Biophysics. His Biochemistry study frequently links to related topics such as Molecular biology. His GroEL research is multidisciplinary, incorporating perspectives in Crystallography, Folding and Cryo-electron microscopy.
His Chaperonin study is focused on Protein folding in general. His GroES research integrates issues from RuBisCO, Cooperativity, Adenosine triphosphate and Nucleotide. The various areas that he examines in his Biophysics study include ATP hydrolysis, ATPase, Plasma protein binding, Chaperone and Allosteric regulation.
The scientist’s investigation covers issues in GroEL, Biophysics, Chaperonin, GroES and Biochemistry. His GroEL research incorporates themes from Folding, Molecular physics, Crystallography and Cryo-electron microscopy. His work deals with themes such as ATP hydrolysis, ATPase, Protein subunit, Chaperone and Allosteric regulation, which intersect with Biophysics.
His Chaperonin study contributes to a more complete understanding of Protein folding. His GroES research incorporates elements of Nucleotide and RuBisCO. The concepts of his Biochemistry study are interwoven with issues in Motor neuron and Cell biology.
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Residues in chaperonin GroEL required for polypeptide binding and release
Fenton Wa;Kashi Y;Furtak K;Horwich Al.
STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING
Paul B. Sigler;Zhaohui Xu;Hays S. Rye;Steven G. Burston.
Annual Review of Biochemistry (1998)
Two Families of Chaperonin: Physiology and Mechanism
Arthur L. Horwich;Wayne A. Fenton;Eli Chapman;George W. Farr.
Annual Review of Cell and Developmental Biology (2007)
Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes
Jonathan S. Weissman;Jonathan S. Weissman;Corinne M. Hohl;Corinne M. Hohl;Oleg Kovalenko;Yechezkel Kashi.
GroEL-mediated protein folding.
Wayne A. Fenton;Arthur L. Horwich.
Protein Science (1997)
Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL
Arthur L. Horwich;K.Brooks Low;Wayne A. Fenton;Irvin N. Hirshfield.
Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction
Jonathan S Weissman;Jonathan S Weissman;Hays S Rye;Hays S Rye;Wayne A Fenton;Joseph M Beechem.
GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
Jonathan S. Weissman;Yechezkel Kashi;Wayne A. Fenton;Arthur L. Horwich.
GroEL-GroES Cycling: ATP and Nonnative Polypeptide Direct Alternation of Folding-Active Rings
Hays S. Rye;Hays S. Rye;Alan M. Roseman;Shaoxia Chen;Krystyna Furtak;Krystyna Furtak.
Structure and expression of a complementary DNA for the nuclear coded precursor of human mitochondrial ornithine transcarbamylase.
Arthur L. Horwich;Wayne A. Fenton;Kenneth R. Williams;Frantisek Kalousek.
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