Conformational and Aggregational Properties of the Gene 9 Minor Coat Protein of Bacteriophage M13 in Membrane-Mimicking Systems

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• 作者：M. Chantal Houbiers ; Ruud B. Spruijt ; Cor J. A. M. Wolfs ; and Marcus A. Hemminga
• 刊名：Biochemistry
• 出版年：1999
• 出版时间：January 19, 1999
• 年：1999
• 卷：38
• 期：3
• 页码：1128 - 1135
• 全文大小：96K
• 年卷期：v.38,no.3(January 19, 1999)
• ISSN：1520-4995

文摘

The membrane-bound state of the gene 9 minor coat protein of bacteriophage M13 was studiedin various membrane-mimicking systems, including organic solvents, detergent micelles, and phospholipidbilayers. For this purpose we determined the conformational and aggregational properties of the chemicallysynthesized protein by CD, FTIR, and HPSEC. The protein appears to be in a monomeric or smalloligomeric mages/gifchars/alpha.gif" BORDER=0>-helical state in TFE but adopts a mixture of mages/gifchars/alpha.gif" BORDER=0>-helical and random structure after subsequentincorporation into SDS or DOPG. When solubilized by sodium cholate, however, the protein undergoesa transition in time into large aggregates, which contain mainly mages/gifchars/beta2.gif" BORDER=0 ALIGN="middle">-sheet conformation. The rate of thismages/gifchars/beta2.gif" BORDER=0 ALIGN="middle">-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. Byreconstitution of the cholate-solubilized protein into DOPG, it was found that the state of the protein,whether initially mages/gifchars/alpha.gif" BORDER=0>-helical monomeric/oligomeric or mages/gifchars/beta2.gif" BORDER=0 ALIGN="middle">-sheet aggregate, did not change. On the basis ofour results, we propose that the principal conformational state of membrane-bound gene 9 protein in vivois mages/gifchars/alpha.gif" BORDER=0>-helical.