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. 2008 Aug 26;3(8):e3063. doi: 10.1371/journal.pone.0003063

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Bhardwaj et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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(A) CD spectra of thermal denaturation of ΔV1, V1L, V1D, V1F, V1A and R-BSX monitored at 222 nm with a temperature slope of 1°C/min. (B) CD spectra of thermal denaturation of V1G and R-BSX, showing the ∼12°C decrease in T_m for V1G. (C) Xylanase activity profile of R-BSX mutants at various temperatures. Maximum activity for V1G was observed at 60°C, differing from other mutants which showed maximum activity at 70°C similar to that of R-BSX. (D) SwissPdb-generated structural models showing the N-terminal region of all R-BSX variants. The amino acid substituted for Val1 is shown in pink. The additional hydrogen bonds resulting from a deletion/substitution are shown in green dotted lines.