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Article

Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder.

Journal of molecular biology - 11 Jul 2008

Nickson Adrian A, Stoll Kate E, Clarke Jane

Abstract excerpt

Protein-engineering methods (Phi-values) were used to investigate the folding transition state of a lysin motif (LysM) domain from Escherichia coli membrane-bound lytic murein transglycosylase D. This domain consists of just 48 structured residues in a symmetrical betaalphaalphabeta arrangement and is the smallest alphabeta protein yet investigated using these methods. An extensive mutational analysis revealed a...

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Identifiers

PMID: 18538343
DOI: 10.1016/j.jmb.2008.05.020
PMCID: PMC2441773

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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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