• Title of article

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

  • Author/Authors

    S. Dyksterhuis، نويسنده , , Leanne B. and Carter، نويسنده , , Elizabeth A. and Mithieux، نويسنده , , Suzanne M. and Weiss، نويسنده , , Anthony S.، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2009
  • Pages
    6
  • From page
    79
  • To page
    84
  • 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.
  • Keywords
    Tropoelastin , intrinsically disordered , Premolten globule , Trimethylamine N-oxide , Thermodynamically unfolded
  • Journal title
    Archives of Biochemistry and Biophysics
  • Serial Year
    2009
  • Journal title
    Archives of Biochemistry and Biophysics
  • Record number

    1630655