Sandbox 179: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Bobbi Piche (talk | contribs) No edit summary |
Bobbi Piche (talk | contribs) No edit summary |
||
| Line 31: | Line 31: | ||
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" /> . | ||
---- | ---- | ||
