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Article

Disulfide bond isomerization in BPTI and BPTI(G36S): an NMR study of correlated mobility in proteins.

Biochemistry - 13 Apr 1993

Otting G, Liepinsh E, Wüthrich K

Abstract excerpt

Two conformational isomers were observed in the 1H nuclear magnetic resonance (NMR) spectra of the basic pancreatic trypsin inhibitor (BPTI) and of a mutant protein with Gly 36 replaced by Ser, BPTI(G36S). The less abundant isomer differs from the major conformation by different chirality of the Cys 14-Cys 38 disulfide bond. In BPTI, the population of the minor conformer increases from about 1.5% at 4 degrees C...

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PMID: 7682109
DOI: 10.1021/bi00065a008

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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