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Article

Hydrogen-exchange behavior of the L20A mutant of the protein A B domain in guanidinium chloride: evidence for persistent native-like contacts.

Scientific reports - 8 Jun 2026

Hayashi Seiichiro, Yanaka Saeko, Yagi-Utsumi Maho, Isono Yukiko, Kato Koichi, Kuwajima Kunihiro

Abstract excerpt

Residual structure in unfolded proteins plays a crucial role in directing folding pathways. Here, we examined the unfolded state of the B domain of staphylococcal protein A carrying the L20A mutation, which disrupts native hydrophobic contacts between Leu20 and helix H3 (residues 41-56). The L20A mutant markedly reduced the thermodynamic stability of the native state. Using dimethylsulfoxide (DMSO)-quenched...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 42259873
DOI: 10.1038/s41598-026-55655-x
PMCID: PMC13476237

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

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