Redesigning the Quaternary Structure of R67 Dihydrofolate Reductase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference36 articles.
1. Design, creation, and characterization of a stable, monomeric triosephosphate isomerase.
2. The crystal structure of an engineered monomeric triosephosphate isomerase, monoTIM: the correct modelling of an eight-residue loop
3. Engineering the quaternary structure of an enzyme: Construction and analysis of a monomeric form of malate dehydrogenase fromEscherichia coli
4. A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site
5. Unusual Binding Stoichiometries and Cooperativity Are Observed during Binary and Ternary Complex Formation in the Single Active Pore of R67 Dihydrofolate Reductase, a D2 Symmetric Protein
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1. From a binding module to essential catalytic activity: how nature stumbled on a good thing;Chemical Communications;2023
2. Small Angle Neutron Scattering Studies of R67 Dihydrofolate Reductase, a Tetrameric Protein with Intrinsically Disordered N-Termini;Biochemistry;2017-10-11
3. Tales of Dihydrofolate Binding to R67 Dihydrofolate Reductase;Biochemistry;2015-12-21
4. Radical Redesign of a Tandem Array of Four R67 Dihydrofolate Reductase Genes Yields a Functional, Folded Protein Possessing 45 Substitutions;Biochemistry;2010-08-04
5. R67, the Other Dihydrofolate Reductase: Rational Design of an Alternate Active Site Configuration;Biochemistry;2007-12-18
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