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Tropoelastin as a thermodynamically unfolded premolten globule protein: The effect of trimethylamine N-oxide on structure and coacervation

  • Leanne B Dyksterhuis
  • , Elizabeth A Carter
  • , Suzanne M Mithieux
  • , Anthony S Weiss

Research output: Contribution to journalArticleResearchpeer-review

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.
Original languageEnglish
Pages (from-to)79 - 84
Number of pages6
JournalArchives of Biochemistry and Biophysics
Volume487
Issue number2
DOIs
Publication statusPublished - 2009
Externally publishedYes

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