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

Archives of Biochemistry and Biophysics

Volumn 487, Issue 2, 2009, Pages 79-84

  Dyksterhuis, Leanne B ^a   Carter, Elizabeth A ^b   Mithieux, Suzanne M ^c   Weiss, Anthony S ^c  

^a CSIRO   (Australia)

^b UNIVERSITY OF SYDNEY   (Australia)

^c UNIVERSITY OF SYDNEY   (Australia)

Author keywords

Intrinsically disordered; Premolten globule; Thermodynamically unfolded; Trimethylamine N oxide; Tropoelastin

Indexed keywords

TRIMETHYLAMINE OXIDE; TROPOELASTIN;

ARTICLE; COACERVATION; HUMAN; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN POLYMERIZATION; PROTEIN STRUCTURE; THERMODYNAMICS;

CIRCULAR DICHROISM; EMULSIONS; HUMANS; METHYLAMINES; PROTEIN BINDING; PROTEIN DENATURATION; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TEMPERATURE; THERMODYNAMICS; TROPOELASTIN;

EID: 67649804607     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2009.06.001     Document Type: Article

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