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Article

Structural determinants of cold adaptation and stability in a large protein.

The Journal of biological chemistry - 13 Jul 2001

D'Amico S, Gerday C, Feller G

Abstract excerpt

The heat-labile alpha-amylase from an antarctic bacterium is the largest known protein that unfolds reversibly according to a two-state transition as shown by differential scanning calorimetry. Mutants of this enzyme were produced, carrying additional weak interactions found in thermostable alpha-amylases. It is shown that single amino acid side chain substitutions can significantly modify the melting point T(m),...

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Identifiers

PMID: 11325973
DOI: 10.1074/jbc.M102741200

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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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