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....Show more
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.