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Article

Protein engineering to improve the thermostability of glucoamylase from Aspergillus awamori based on molecular dynamics simulations.

Protein engineering - 1 Jan 2003

Liu Hsuan-Liang, Wang Wen-Chi

Abstract excerpt

Twelve mutations were constructed to improve the thermostability of glucoamylase from Aspergillus awamori based on the results of molecular dynamics simulations. The thermal unfolding of the catalytic domain followed a putative hierarchical behavior. In addition, the unfolding of the 13 alpha-helices obeyed the random ordered mechanism, in which the alpha-helices 8, 1 and 11 unfolded more rapidly than the others....

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Identifiers

PMID: 12646689
DOI: 10.1093/proeng/gzg007

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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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