![]() Gao, Kai Beijing Key Laboratory of Noncoding RNA, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101 University of Chinese Academy of Sciences, Beijing 100049Įnveloped virus, such as HIV-1, employs membrane fusion mechanism to invade into host cell. PMID:12142459Įxploring the membrane fusion mechanism through force- induced disassembly of HIV-1 six- helix bundle Together these results support the tenets of the osmophobic hypothesis and highlight the importance of the polypeptide backbone in protein folding and stability. Finally, we extend the investigations to the effects of urea and TMAO on the stability of a dimeric coiled-coil peptide and find identical results. We find that on a molar basis, these agents are exactly counteractive as structure inducing and unfolding agents. We also provide a semiquantitative study of the ability of TMAO to induce helix formation and urea, which acts as a helix (and protein) denaturant. Trimethylamine-N-oxide (TMAO) is the best structure- inducing osmolytes investigated here, but it is not as effective in promoting helix formation as the common cosolvent trifluoroethanol (TFE). As predicted by the osmophobic effect hypothesis, the osmolytes studies here do induce helix formation. The ability of several naturally occurring substances known as osmolytes to induce helix formation in an alanine-based peptide have been investigated. Osmolyte effects on helix formation in peptides and the stability of coiled-coils
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