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
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
Journal title :
Archives of Biochemistry and Biophysics