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

Enhancing the thermal stability of a single-chain Fv fragment by in vivo global fluorination of the proline residues

19 Nov 2010

Abstract excerpt

Single-chain Fv (scFv) format protein is a commonly used analytical tool for diagnostic and therapeutic applications. The usage of scFv antibody fragments in therapeutic applications has demonstrated that they need to have high thermostability. Many rational or irrational methods have been described erstwhile to engineer or improve the stability of scFv proteins by modifications of natural amino acid. Here we...

Read the complete abstract on PubMed

Topics

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

Share to Glycosylation and Glycoproteins Research
Share to Monoclonal and Polyclonal Antibodies Research
Share to Protein purification and stability

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 21103487
DOI: 10.1039/c0mb00154f

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Enhancing the thermal stability of a single-chain Fv fragment by in vivo global fluorination of the proline residuesPMID 21103487Read ↗

Residue-specific bioincorporation of non-natural, biologically active amino acids into proteins as possible drug carriers: structure and stability of the per-thiaproline mutant of annexin V.Semantic proximity Read ↗

Proline-Mediated Enhancement in Evolvability of Disulfide-Rich Peptides for Discovering Protein BindersSemantic proximity Read ↗

Stability engineering of antibody single-chain Fv fragments.Semantic proximity Read ↗

Engineering stability into Escherichia coli secreted Fabs leads to increased functional expression.Semantic proximity Read ↗

Strategy of selection and optimization of single domain antibodies targeting the PHF6 linear peptide within the Tau intrinsically disordered proteinSemantic proximity Read ↗

A selection and optimization strategy for single-domain antibodies targeting the PHF6 linear peptide within the tau intrinsically disordered proteinSemantic proximity Read ↗

Stabilization of bzip peptides through incorporation of fluorinated aliphatic residues.Semantic proximity Read ↗

Efficient isolation of soluble intracellular single-chain antibodies using the twin-arginine translocation machinery.Semantic proximity Read ↗

The VH framework region 1 as a target of efficient mutagenesis for generating a variety of affinity-matured scFv mutantsSemantic proximity Read ↗

Helix-stabilized Fv (hsFv) antibody fragments: substituting the constant domains of a Fab fragment for a heterodimeric coiled-coil domain.Semantic proximity Read ↗

Rational design of environmentally responsive antibodies with pH-sensing synthetic amino acidsSemantic proximity Read ↗

Genetic Encoding of A Nonhydrolyzable Phosphotyrosine Analog in Mammalian CellsSemantic proximity Read ↗

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