Redesigning the Quaternary Structure of R67 Dihydrofolate Reductase - Wikidata - awgldk - TriplyDB

Redesigning the Quaternary Structure of R67 Dihydrofolate Reductase

Redesigning the Quaternary Structure of R67 Dihydrofolate Reductase

http://www.wikidata.org/entity/Q58322383

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Role of Lys-32 residues in R67 dihydrofolate reductase probed by asymmetric mutations."Catch 222," the effects of symmetry on ligand binding and catalysis in R67 dihydrofolate reductase as determined by mutations at Tyr-69.

P2860

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P2860

Redesigning the Quaternary Structure of R67 Dihydrofolate Reductase

http://www.wikidata.org/entity/Q58322383

description

article publié dans la revue scientifique Journal of Biological Chemistry

@fr

im November 1996 veröffentlichter wissenschaftlicher Artikel

@de

scientific article published in Journal of Biological Chemistry

@en

wetenschappelijk artikel

@nl

наукова стаття, опублікована в листопаді 1996

@uk

name

Redesigning the Quaternary Structure of R67 Dihydrofolate Reductase

@en

Redesigning the Quaternary Structure of R67 Dihydrofolate Reductase

@nl

type

label

Redesigning the Quaternary Structure of R67 Dihydrofolate Reductase

@en

Redesigning the Quaternary Structure of R67 Dihydrofolate Reductase

@nl

prefLabel

Redesigning the Quaternary Structure of R67 Dihydrofolate Reductase

@en

Redesigning the Quaternary Structure of R67 Dihydrofolate Reductase

@nl

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P356

JBC.271.45.28031

P1433

Journal of Biological Chemistry

P1476

Redesigning the quaternary str ...... by quadruplication of the gene

@en

P2093

C Shattuck

http://www.w3.org/2001/XMLSchema#string

C Wicker

http://www.w3.org/2001/XMLSchema#string

E Eisenstein

http://www.w3.org/2001/XMLSchema#string

M B Strader

http://www.w3.org/2001/XMLSchema#string

T D Bradrick

http://www.w3.org/2001/XMLSchema#string

P2860

A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site

Purification and properties of Escherichia coli dihydrofolate reductase.

Construction of a synthetic gene for an R-plasmid-encoded dihydrofolate reductase and studies on the role of the N-terminus in the protein.

Crystal structure of a novel trimethoprim-resistant dihydrofolate reductase specified in Escherichia coli by R-plasmid R67.

Stability and activity of human immunodeficiency virus protease: comparison of the natural dimer with a homologous, single-chain tethered dimer.

Engineering the quaternary structure of an enzyme: construction and analysis of a monomeric form of malate dehydrogenase from Escherichia coli.

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.

Design, creation, and characterization of a stable, monomeric triosephosphate isomerase.

Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutants.

Communication between catalytic subunits in hybrid aspartate transcarbamoylase molecules: effect of ligand binding to active chains on the conformation of unliganded, inactive chains.

P304

28031-28037

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P31

scholarly article

P356

10.1074/JBC.271.45.28031

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P407

P433

45

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P478

271

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P50

Elizabeth Howell

P577

1996-11-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

8910413

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