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Article

NMR structural study of two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]--a disulfide intermediate with a partly unfolded structure.

Biochemistry - 19 Feb 2002

Noda Yasuo, Yokota Atsushi, Horii Daisuke, Tominaga Takeshi, Tanisaka Yoshiaki, Tachibana Hideki, Segawa Shin-ichi

Abstract excerpt

The 15N-labeled recombinant hen lysozyme and two species of two-disulfide variants, denoted as 2SS[6-127, 30-115] and 2SS[64-80, 76-94], were studied by means of NMR spectroscopy. The former variant contains two disulfide bridges in the alpha-domain, while the latter has one disulfide bridge in the beta-domain and the other one at the interface between two domains. Resonance assignments were performed using 3D...

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PMID: 11841203
DOI: 10.1021/bi0113418

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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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