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Article

The effects of an ideal beta-turn on beta-2 microglobulin fold stability.

Journal of biochemistry - 1 Jul 2011

Colombo Matteo, Ricagno Stefano, Barbiroli Alberto, Santambrogio Carlo, Giorgetti Sofia, Raimondi Sara, Bonomi Francesco, Grandori Rita, Bellotti Vittorio, Bolognesi Martino

Abstract excerpt

Beta-2 microglobulin (β2m) is the light chain of Class I major histocompatibility complex (MHC-I) complex. β2m is an intrinsically amyloidogenic protein capable of forming amyloid fibrils in vitro and in vivo. β2m displays the typical immunoglobulin-like fold with a disulphide bridge (Cys25-Cys80) cross-linking the two β-sheets. Engineering of the loop comprised between β-strands D and E has shown that mutations...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 21398368
DOI: 10.1093/jb/mvr034

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

Source receipt: pubmed, retrieved 7 Sept 2026.

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