Flow Linear Dichroism of Some Prototypical Proteins

Autor: Timothy R. Dafforn, Alison Rodger, Matthew R. Hicks, Jonathan D. Hirst, Benjamin M. Bulheller, Patrick J. S. King, Kevin J. Channon, Louise C. Serpell, Karen E. Marshall, Elizabeth H. C. Bromley, Derek N. Woolfson
Rok vydání: 2009
Předmět:
Zdroj: Journal of the American Chemical Society. 131:13305-13314
ISSN: 1520-5126
0002-7863
DOI: 10.1021/ja902662e
Popis: Flow linear dichroism (LD) spectroscopy provides information on the orientation of molecules in solution and hence on the relative orientation of parts of molecules. Long molecules such as fibrous proteins can be aligned in Couette flow cells and characterized using LD. We have measured using Couette flow and calculated from first principles the LD of proteins representing prototypical secondary structure classes: a self-assembling fiber and tropomyosin (all-alpha-helical), FtsZ (an alphabeta protein), an amyloid fibril (beta-sheet), and collagen [poly(proline)II helices]. The combination of calculation and experiment allows elucidation of the protein orientation in the Couette flow and the orientation of chromophores within the protein fibers.
Databáze: OpenAIRE