Conformational and aggregational properties of the gene 9 minor coat protein of bacteriophage M13 in membrane-mimicking systems
Biochemistry, ISSN: 0006-2960, Vol: 38, Issue: 3, Page: 1128-1135
1999
- 8Citations
- 13Captures
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Metrics Details
- Citations8
- Citation Indexes8
- CrossRef8
- Captures13
- Readers13
- 13
Article Description
The membrane-bound state of the gene 9 minor coat protein of bacteriophage M13 was studied in various membrane-mimicking systems, including organic solvents, detergent micelles, and phospholipid bilayers. For this purpose we determined the conformational and aggregational properties of the chemically synthesized protein by CD, FTIR, and HPSEC. The protein appears to be in a monomeric or small oligomeric α-helical state in TFE but adopts a mixture of α-helical and random structure after subsequent incorporation into SDS or DOPG. When solubilized by sodium cholate, however, the protein undergoes a transition in time into large aggregates, which contain mainly β-sheet conformation. The rate of this β-polymerization process was decreased at lower temperature and higher concentrations of sodium cholate. This aggregation was reversed only upon addition of high concentrations of the strong detergent SDS. By reconstitution of the cholate- solubilized protein into DOPG, it was found that the state of the protein, whether initially α-helical monomeric/oligomeric or β-sheet aggregate, did not change. On the basis of our results, we propose that the principal conformational state of membrane-bound gene 9 protein in vivo is α-helical.
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