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 |
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Rok vydání: | 2009 |
Předmět: |
Models
Molecular biology Chemistry Spectrum Analysis Proteins General Chemistry Chromophore Linear dichroism Biochemistry Tropomyosin Protein Structure Secondary Catalysis Crystallography Colloid and Surface Chemistry biology.protein Molecule Fiber Protein Multimerization Protein Structure Quaternary FtsZ Protein secondary structure Couette flow |
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 |
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