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Updated: Jun 22, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Tropoelastin as a thermodynamically unfolded premolten globule protein: The effect of trimethylamine N-oxide on
Leanne B Dyksterhuis1, Elizabeth A Carter, Suzanne M Mithieux
1CSIRO Molecular and Health Technologies, Clayton, Vic. 3168, Australia. Leanne.Dyksterhuis@csiro.au
Abstract:
Tropoelastin is the monomer building block of the biopolymer elastin, which is responsible for elasticity in arteries, lung and skin. Previous studies have shown that, in contrast to predictions made based on primary sequence, tropoelastin has little regular secondary structure in aqueous solution and displays considerable flexibility. This investigation defines the level of residual structure present in tropoelastin and uses the naturally-occurring structure-inducing osmolyte trimethylamine N-oxide to examine the potential for regular structure in tropoelastin. Tropoelastin is defined as a thermodynamically unfolded premolten globule, which can account for its ability to elastically deform.
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