the critical role of partially exposed n-terminal valine residue in stabilizing gh10 xylanase from bacillus sp.ng-27 under poly-extreme conditions部分暴露的氨基端缬氨酸残基的关键作用在稳定gh10木聚糖酶的芽孢杆菌sp.ng-27 poly-extreme条件下.pdfVIP

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the critical role of partially exposed n-terminal valine residue in stabilizing gh10 xylanase from bacillus sp.ng-27 under poly-extreme conditions部分暴露的氨基端缬氨酸残基的关键作用在稳定gh10木聚糖酶的芽孢杆菌sp.ng-27 poly-extreme条件下.pdf

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the critical role of partially exposed n-terminal valine residue in stabilizing gh10 xylanase from bacillus sp.ng-27 under poly-extreme conditions部分暴露的氨基端缬氨酸残基的关键作用在稳定gh10木聚糖酶的芽孢杆菌sp.ng-27 poly-extreme条件下

The Critical Role of Partially Exposed N-Terminal Valine Residue in Stabilizing GH10 Xylanase from Bacillus sp. NG-27 under Poly-Extreme Conditions 1,2 1 2 3 Amit Bharadwaj , Sadhu Leelavathi , Sudeshna Mazumdar-Leighton , Amit Ghosh , Suryanarayanarao 4,5 1 Ramakumar , Vanga S. Reddy * 1 International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg, New Delhi, India, 2 Department of Botany, University of Delhi, Delhi, India, 3 Indian Institute of Advanced Research, Gandhinagar, India, 4 Department of Physics, Indian Institute of Science, Bangalore, India, 5 Bioinformatics Centre, Indian Institute of Science, Bangalore, India Abstract Background: Understanding the mechanisms that govern protein stability under poly-extreme conditions continues to be a major challenge. Xylanase (BSX) from Bacillus sp. NG-27, which has a TIM-barrel structure, shows optimum activity at high temperature and alkaline pH, and is resistant to denaturation by SDS and degradation by proteinase K. A comparative circular dichroism analysis was performed on native BSX and a recombinant BSX (R-BSX) with just one additional methionine resulting from the start codon. The results of this analysis revealed the role of the partially exposed N-terminus in the unfolding of BSX in response to an increase in temperature. Methodology: We investigated the poly-extremophilicity of BSX to deduce the structural features responsible for its stability under one set of conditions, in order to gain information about its stability in other extreme conditions. To systematically address the role of the partially exposed N-terminus in BSX stability, a series of mutants was gene