Conformational preludes to the latency transition in PAI-1 as determined by atomistic computer simulations and hydrogen/deuterium-exchange mass spectrometry
Abstract Both function and dysfunction of serine protease inhibitors (serpins) involve massive conformational change in their tertiary structure but the dynamics facilitating these events remain poorly understood. We have studied the dynamic preludes to conformational change in the serpin plasminoge...
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Autores principales: | , , , |
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Formato: | article |
Lenguaje: | EN |
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Nature Portfolio
2017
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Materias: | |
Acceso en línea: | https://doaj.org/article/2be4f4e67be6467ca11b18fe2c3a033a |
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