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

Automated high-throughput process for site-directed mutagenesis, production, purification, and kinetic characterization of enzymes.

Analytical biochemistry - 1 Aug 2006

Carapito Raphaël, Gallet Benoit, Zapun André, Vernet Thierry

Abstract excerpt

Site-directed mutagenesis followed by functional characterization is a widely used approach to obtain information on the structure-function relationship of proteins. Due to time and cost considerations, the number of amino acids studied is frequently reduced. To address the need for convenient parallel production of numerous point mutants of a protein, we developed an automated method to perform classical...

Read the complete abstract on PubMed

Topics

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

Share to Enzymes
Share to Escherichia coli
Share to Kinetics

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

Share to Mutagenesis, Site-Directed

Share to Mutant Proteins

Share to Penicillin-Binding Proteins

Share to Recombinant Proteins

Share to Reproducibility of Results

Source

Identifiers

PMID: 16797473
DOI: 10.1016/j.ab.2006.04.047

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Automated high-throughput process for site-directed mutagenesis, production, purification, and kinetic characterization of enzymes.PMID 16797473Read ↗

Pneumococcal beta-lactam resistance due to a conformational change in penicillin-binding protein 2x.Semantic proximity Read ↗

A PBP2x from a clinical isolate of Streptococcus pneumoniae exhibits an alternative mechanism for reduction of susceptibility to beta-lactam antibiotics.Semantic proximity Read ↗

The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: implication in drug resistance.Semantic proximity Read ↗

Increasing the synthetic performance of penicillin acylase PAS2 by structure-inspired semi-random mutagenesis.Semantic proximity Read ↗

Site-saturation mutagenesis: a powerful tool for structure-based design of combinatorial mutation libraries.Semantic proximity Read ↗

Practical Considerations Regarding the Choice of the Best High-Throughput Assay.Semantic proximity Read ↗

Deep mutational scanning of essential bacterial proteins can guide antibiotic development.Semantic proximity Read ↗

Improved bacterial recombineering by parallelized protein discovery.Semantic proximity Read ↗

Crystal structure of PBP2x from a highly penicillin-resistant Streptococcus pneumoniae clinical isolate: a mosaic framework containing 83 mutations.Semantic proximity Read ↗

Multiplex site-directed mutagenesis strategy including high-efficiency selection of the mutant PCR products.Semantic proximity Read ↗

Protein engineering.Semantic proximity Read ↗

A Brief Guide to the High-Throughput Expression of Directed Evolution Libraries.Semantic proximity Read ↗

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