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May 2009

Volume 8Issue 5p883-1166
Open Access
On the cover: Functional unfolding of α1-antitrypsin (a member of serpin family) was probed by H/D-exchange and ESI-MS. The native α1-antitrypsin, a kinetically trapped folding intermediate, unfolds transiently during complex formation with a target protease, which is critical for execution of protease inhibition. For details, see the article by Baek et al., pages 1072–1081....
On the cover: Functional unfolding of α1-antitrypsin (a member of serpin family) was probed by H/D-exchange and ESI-MS. The native α1-antitrypsin, a kinetically trapped folding intermediate, unfolds transiently during complex formation with a target protease, which is critical for execution of protease inhibition. For details, see the article by Baek et al., pages 1072–1081.

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