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

Increasing the melting temperature of VHH with the in silico free energy score.

Scientific reports - 25 Mar 2023

Tomimoto Yusuke, Yamazaki Rika, Shirai Hiroki

Abstract excerpt

VHH, the antigen-binding fragment of a heavy chain-only antibody, is a useful component of antibody-based therapeutics. Thermal stability, represented by the melting temperature (Tm), is one of the key factors affecting the developability of antibody-based therapeutics. In this study, we examined whether the in silico free energy score dStability can be used to design mutants with improved Tm compared to the...

Read the complete abstract on PubMed

Topics

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

Share to Antibodies
Share to Entropy
Share to Mutagenesis

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

Share to Mutation

Share to Temperature

Source

Open in PubMed Open full text

Identifiers

PMID: 36966210
DOI: 10.1038/s41598-023-32022-8
PMCID: PMC10039853

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

Increasing the melting temperature of VHH with the in silico free energy score.PMID 36966210Read ↗

Thermodynamics of antibody-antigen interaction revealed by mutation analysis of antibody variable regions.Semantic proximity Read ↗

An optimized thermodynamics integration protocol for identifying beneficial mutations in antibody design.Semantic proximity Read ↗

Improving antibody thermostability based on statistical analysis of sequence and structural consensus dataSemantic proximity Read ↗

Enhancement of Protein-Protein Interactions by Destabilizing Mutations Revealed by HDX-MS.Semantic proximity Read ↗

Assessment of software methods for estimating protein-protein relative binding affinities.Semantic proximity Read ↗

Analysis of how antigen mutations disrupt antibody binding interactions toward enabling rapid and reliable antibody repurposing.Semantic proximity Read ↗

Accurate Prediction of Protein Thermodynamic Stability Changes upon Residue Mutation using Free Energy Perturbation.Semantic proximity Read ↗

Contributions of the complementarity determining regions to the thermal stability of a single-domain antibody.Semantic proximity Read ↗

Role of simple descriptors and applicability domain in predicting change in protein thermostability.Semantic proximity Read ↗

Lessons learned from merging wet lab experiments with molecular simulation to improve mAb humanization.Semantic proximity Read ↗

Computational design of antibody-affinity improvement beyond in vivo maturation.Semantic proximity Read ↗

Affinity improvement of a therapeutic antibody by structure-based computational design: generation of electrostatic interactions in the transition state stabilizes the antibody-antigen complex.Semantic proximity Read ↗

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