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Article

Remarkable improvement of methylglyoxal synthase thermostability by His-His interaction.

Applied biochemistry and biotechnology - 1 Jan 2014

Mohammadi Malihe, Kashi Mona Atabakhshi, Zareian Shekufeh, Mirshahi Manoochehr, Khajeh Khosro

Abstract excerpt

Lately it has been proposed that interaction between two positively charged side chains can stabilize the folded state of proteins. To further explore this point, we studied the effect of histidine-histidine interactions on thermostability of methylglyoxal synthase from Thermus sp. GH5 (TMGS). The crystal structure of TMGS revealed that His23, Arg22, and Phe19 are in close distance and form a surface loop. Here,...

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PMID: 24057302
DOI: 10.1007/s12010-013-0404-y

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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