Marie Julie Boulanger, Rollenbild, Brustbild, Opéra Comique

Signatur des Originals: S 36/G00525

Marie Julie Boulanger, Rollenbild, Brustbild, Paris: Opéra Comique

Signatur des Originals: S 36/G00526

Marie Julie Boulanger, Rollenbild, Brustbild, Paris: Opéra Comique

Signatur des Originals: S 36/G00527

Julie Aimée Joseph Gras-Dorus, Hüftbild

Signatur des Originals: S 36/G00738

Julie Aimée Joseph Gras-Dorus als Marguerite de Valois, Rollenbild, Hüftbild, in: Giacomo Meyerbeer: Les Huguenots

Signatur des Originals: S 36/G00740

Julie Dumont-Suvanny, Kniestück

Signatur des Originals: S 36/G00749

Julie Koch-Bossenberger, Hüftbild, Profil

Signatur des Originals: S 36/G01310

Julie Koch-Bossenberger, Hüftbild, Profil

Signatur des Originals: S 36/G01311

Julie Rettich, Hüftbild

Signatur des Originals: S 36/G02009

Marie Julie Boulanger, Rollenbild, Brustbild, in: Pierre-Alexandre Monsigny: Aline, reine de Golconde

Signatur des Originals: S 36/G03953

Julie Aimée Joseph Gras-Dorus, Rollenbild, Kniestück

Signatur des Originals: S 36/G04008

Interview with Julie Knobil

An oral interview with Juile (Hotchkiss) Knobil, research professor of physiology and then integrative biology at the Medical School, where she lectured on mammalian physiology and perinatal endocrinology.

Kinetic stability as a mechanism for protease longevity

The folding of the extracellular serine protease, α-lytic protease (αLP; EC 3.4.21.12) reveals a novel mechanism for stability that appears to lead to a longer functional lifetime for the protease. For αLP, stability is based not on thermodynamics, but on kinetics. Whereas this has required the coevolution of a pro region to facilitate folding, the result has been the optimization of native-state properties independent of their consequences on thermodynamic stability. Structural and mutational data lead to a model for catalysis of folding in which the pro region binds to a conserved β-hairpin in the αLP C-terminal domain, stabilizing the folding transition state and the native state. The pro region is then proteolytically degraded, leaving the active αLP trapped in a metastable conformation. This metastability appears to be a consequence of pressure to evolve properties of the native state, including a large, highly cooperative barrier to unfolding, and extreme rigidity, that reduce susceptibility to proteolytic degradation. In a test of survival under highly proteolytic conditions, homologous mammalian proteases that have not evolved kinetic stability are much more rapidly degraded than αLP. Kinetic stability as a means to longevity is likely to be a mechanism conserved among the majority of extracellular bacterial pro-proteases and may emerge as a general strategy for intracellular eukaryotic proteases subject to harsh conditions as well.