Tropoelastin as a thermodynamically unfolded premolten globule protein: The effect of trimethylamine N-oxide on structure and coacervation
| Autor: | Elizabeth A. Carter, Leanne B Dyksterhuis, Suzanne M. Mithieux, Anthony S. Weiss |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Circular dichroism
Protein Denaturation Biophysics Trimethylamine Trimethylamine N-oxide Biochemistry chemistry.chemical_compound Methylamines Tropoelastin Spectroscopy Fourier Transform Infrared Humans Molecular Biology Protein secondary structure Coacervate integumentary system biology Circular Dichroism Temperature Monomer chemistry biology.protein Thermodynamics Emulsions Elastin Protein Binding |
| Zdroj: | Archives of biochemistry and biophysics. 487(2) |
| ISSN: | 1096-0384 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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