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. 2010 Oct 28;6(10):e1001168. doi: 10.1371/journal.ppat.1001168

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This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.

This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.

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Ala463-to-Ile, Gln479-to-Lys and Lys480-to-Ile mutations (in the HPIV3 F HRC region) stabilize the heterotypic six-helix bundle structure formed by the recombinant N42_NiV(L6)C32_HPIV3-V model. (A) Circular dichroism (CD) spectrum of N42_NiV(L6)C32_HPIV3-VIKI (50 uM) in TBS (pH 8.0) at 4°C. (B) Thermal melts of N42_NiV(L6)C32_HPIV3-VIKI monitored by CD at 222 nm at 50 uM protein concentration in TBS (pH 8.0) in the presence (open circles) and absence (filled circles) of 3 M GuHCl, a chemical denaturant. (C) Representative sedimentation equilibrium data (19 krpm) of N42_NiV(L6)C32_HPIV3-VIKI collected at 20°C in TBS (pH 8.0) at ∼30 uM protein concentration. The natural logarithm of the absorbance at 273 nm is plotted against the square of the radial position. The random distributions of the residuals indicate that the data fit well to an ideal single-species model. The slope of the plotted data indicates that N42_NiV(L6)C32_HPIV3-VIKI is a trimer.