(Q57905137)

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Direct observation by NMR of two coexisting conformations of an enzyme–ligand complex in solution

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title

Direct observation by NMR of two coexisting conformations of an enzyme–ligand complex in solution (English)

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author name string

A. Gronenborn

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1

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B. Birdsall

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2

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E. I. Hyde

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3

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G. C. K. Roberts

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4

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J. Feeney

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5

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A. S. V. Burgen

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6

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English

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publication date

March 1981

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Nature

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volume

290

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issue

5803

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page(s)

273-274

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exact match

https://scigraph.springernature.com/pub.10.1038/290273a0

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cites work

Binding of coenzyme analogues to Lactobacillus casei dihydrofolate reductase: binary and ternary complexes.

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7 January 2021

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Proton nuclear magnetic resonance saturation transfer studies of coenzyme binding to Lactobacillus casei dihydrofolate reductase.

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7 January 2021

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Phosphorus-31 nuclear magnetic resonance studies of the binding of oxidized coenzymes to Lactobacillus casei dihydrofolate reductase.

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7 January 2021

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Photo-CIDNP studies of the influence of ligand binding on the surface accessibility of aromatic residues in dihydrofolate reductase.

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Cooperativity in ligand binding to dihydrofolate reductase

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Amino acid sequence of dihydrofolate reductase from an amethopterin-resistant strain ofLactobacillus casei

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7 January 2021

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Histidine residues of Lactobacillus casei dihydrofolate reductase: paramagnetic relaxation and deuterium-exchange studies and partial assignments

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7 January 2021

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Escherichia coli dihydrofolate reductase: isolation and characterization of two isozymes

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7 January 2021

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Nuclear magnetic resonance studies of the binding of trimethoprim to dihydrofolate reductase

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https://api.crossref.org/works/10.1038%2F290273A0

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7 January 2021

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DOI

10.1038/290273A0

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1001042524

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(Q57905137)

Direct observation by NMR of two coexisting conformations of an enzyme–ligand complex in solution

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