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Article

Nuclear magnetic resonance characterization of the refolding intermediate of beta2-microglobulin trapped by non-native prolyl peptide bond.

Journal of molecular biology - 29 Apr 2005

Kameda Atsushi, Hoshino Masaru, Higurashi Takashi, Takahashi Satoshi, Naiki Hironobu, Goto Yuji

Abstract excerpt

beta(2)-Microglobulin (beta2-m), a light chain of the major histocompatibility complex type I, is also found as a major component of amyloid fibrils formed in dialysis-related amyloidosis. Denaturation of beta2-m is considered to initiate the formation of fibrils. To clarify the mechanism of fibril formation, it is important to characterize the intermediate conformational states at the atomic level. Here, we...

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Identifiers

PMID: 15811375
DOI: 10.1016/j.jmb.2005.02.050

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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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