Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Nonadditive effects of double mutations at the flexible loops, glycine-67 and glycine-121, of Escherichia coli dihydrofolate reductase on its stability and function.

Journal of biochemistry - 1 Jan 1998

Ohmae E, Iriyama K, Ichihara S, Gekko K

Abstract excerpt

The structure, stability, and enzymatic function of dihydrofolate reductase (DHFR) from Escherichia coli are influenced by point mutations at sites 67 and 121 in two flexible loops [Gekko et al. (1994) J. Biochem. 116, 34-41; Ohmae et al. (1996) J. Biochem. 119, 703-710]. In the present study, eight double mutants at sites 67 and 121 (G67V/G121S, G67V/G121A, G67V/G121C, G67V/G121D, G67V/G121V, G67V/G121H,...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Enzyme Stability
Share to Escherichia coli

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Glycine

Share to Kinetics

Share to Mutation

Share to Protein Conformation

Share to Protein Folding

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 9504406
DOI: 10.1093/oxfordjournals.jbchem.a021913

Genes

DHFR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Nonadditive effects of double mutations at the flexible loops, glycine-67 and glycine-121, of Escherichia coli dihydrofolate reductase on its stability and function.PMID 9504406Read ↗

Effects of a distal mutation on active site chemistry.Semantic proximity Read ↗

A distal mutation perturbs dynamic amino acid networks in dihydrofolate reductase.Semantic proximity Read ↗

Evolutional design of a hyperactive cysteine- and methionine-free mutant of Escherichia coli dihydrofolate reductase.Semantic proximity Read ↗

Vacuum-Ultraviolet Circular Dichroism Spectra of Escherichia coli Dihydrofolate Reductase and Its Mutants: Contributions of Phenylalanine and Tyrosine Side Chains and Exciton Coupling of Two Tryptophan Side Chains.Semantic proximity Read ↗

Refolding of human beta-1-2 GlcNAc transferase (GnT1) and the role of its unpaired Cys 121.Semantic proximity Read ↗

Molecular basis for nonadditive mutational effects in Escherichia coli dihydrofolate reductase.Semantic proximity Read ↗

P61A mutation in the factor for inversion stimulation results in a thermostable dimeric intermediate.Semantic proximity Read ↗

Cooperative unfolding of Escherichia coli ribosome recycling factor originating from its domain-domain interaction and its implication for function.Semantic proximity Read ↗

The coupling of structural fluctuations to hydride transfer in dihydrofolate reductase.Semantic proximity Read ↗

Construction and characterization of a single polypeptide chain containing two enzymatically active dihydrofolate reductase domains.Semantic proximity Read ↗

Effect of dimerization on the stability and catalytic activity of dihydrofolate reductase from the hyperthermophile Thermotoga maritima.Semantic proximity Read ↗

Protein motions during catalysis by dihydrofolate reductases.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.