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Article

Conformational stabilization of an engineered binding protein.

Journal of the American Chemical Society - 14 Jun 2006

Wahlberg Elisabet, Härd Torleif

Abstract excerpt

We analyzed the thermodynamic basis for improvement of a binding protein by disulfide engineering. The Z(SPA)(-)(1) affibody binds to its Z domain binding partner with a dissociation constant K(d) = 1.6 microM, and previous analyses suggested that the moderate affinity is due to the conformational heterogeneity of free Z(SPA)(-)(1) rather than to a suboptimal binding interface. Studies of five stabilized...

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Identifiers

PMID: 16756322
DOI: 10.1021/ja060933g

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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