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Article

Directed evolution of human heavy chain variable domain (VH) using in vivo protein fitness filter.

PloS one - 1 Jan 2014

Kim Dong-Sik, Song Hyung-Nam, Nam Hyo Jung, Kim Sung-Geun, Park Young-Seoub, Park Jae-Chan, Woo Eui-Jeon, Lim Hyung-Kwon

Abstract excerpt

Human immunoglobulin heavy chain variable domains (VH) are promising scaffolds for antigen binding. However, VH is an unstable and aggregation-prone protein, hindering its use for therapeutic purposes. To evolve the VH domain, we performed in vivo protein solubility selection that linked antibiotic resistance to the protein folding quality control mechanism of the twin-arginine translocation pathway of E. coli....

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Share to Biophysical Phenomena
Share to Complementarity Determining Regions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Directed Molecular Evolution

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Source

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Identifiers

PMID: 24892548
DOI: 10.1371/journal.pone.0098178
PMCID: PMC4043505

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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