Pepsin: Difference between revisions
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Once denatured, pepsin is unable to refold to an active native state upon returning from denaturing conditions. One proposed solution for this is that pepsin formation depends on a separate prosegment (PS) domain. When returning from the denatured state, the denatured pepsin first has to bypass a large folding barrier and then in the presence of PS the native state can become thermodynamically stable. The PS therefore can catalyze pepsin folding by stabilizing the transition state <ref name="native" /> . | Once denatured, pepsin is unable to refold to an active native state upon returning from denaturing conditions. One proposed solution for this is that pepsin formation depends on a separate prosegment (PS) domain. When returning from the denatured state, the denatured pepsin first has to bypass a large folding barrier and then in the presence of PS the native state can become thermodynamically stable. The PS therefore can catalyze pepsin folding by stabilizing the transition state <ref name="native" /> . | ||
==3D structures of pepsin== | ==3D structures of pepsin== | ||
''Updated December 2011'' | |||
===Pepsin=== | ===Pepsin=== | ||
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[[2ifr]], [[2ifw]], [[1s2k]] – SlPep + peptide<br /> | [[2ifr]], [[2ifw]], [[1s2k]] – SlPep + peptide<br /> | ||
[[1yx9]] – pPep + DMSO<br /> | [[1yx9]] – pPep + DMSO<br /> | ||
[[1psa]] – pPep + inhibitor<br /> | [[1psa]], [[1f34]] – pPep + inhibitor<br /> | ||
[[1wkr]] - Pep + pepstatin – ''Irpex lacteus''<br /> | [[1wkr]] - Pep + pepstatin – ''Irpex lacteus''<br /> | ||
[[4apr]], [[5apr]], [[6apr]] - RcPep + pepstatin<br /> | [[4apr]], [[5apr]], [[6apr]] - RcPep + pepstatin<br /> | ||