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Article

Effects of His mutations on the fibrillation of amyloidogenic Vlambda6 protein Wil under acidic and physiological conditions.

Biochemical and biophysical research communications - 1 Jan 2010

Mishima Tomonori, Ohkuri Takatoshi, Monji Akira, Kanemaru Takaaki, Abe Yoshito, Ueda Tadashi

Abstract excerpt

Recently, we showed that the recombinant (r) Vlambda6 protein Wil exhibits a more disrupted residual structure and a longer lag time for fibril formation than the rVlambda6 protein Jto under highly unfolding conditions at pH 2. Here, we focused on the roles of three histidine residues specific for Wil, which are positively charged at pH 2 and could repel one another. Heteronuclear relaxation experiments revealed...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 19932684
DOI: 10.1016/j.bbrc.2009.11.108

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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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