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Article

Comprehensive analysis of surface charged residues involved in thermal stability in Alicyclobacillus acidocaldarius esterase 2.

Protein engineering, design & selection : PEDS - 1 Jan 2013

Pezzullo Margherita, Del Vecchio Pompea, Mandrich Luigi, Nucci Roberto, Rossi Mosè, Manco Giuseppe

Abstract excerpt

Here we report a comprehensive analysis through alanine-scanning mutagenesis of the contribution of surface ion pairs to the thermal stability of Alicyclobacillus acidocaldarius esterase 2 (EST2). We produced 16 single mutants, 4 double mutants corresponding to selected ion pairs R31/E118, E43/K102, R58/D130, D145/R148, 2 double mutants (R63A/R98A and E50A/D94A) involving residues of a large ion network on the...

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PMID: 23035254
DOI: 10.1093/protein/gzs066

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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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