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- 2Chemical cleavage
- 2Escherichia coli
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- 2Medicine and Dentistry, Faculty of
- 2Medicine and Dentistry, Faculty of/Journal Articles (Medicine and Dentistry)
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Combining a PagP fusion protein system with nickel ion-catalyzed cleavage to produce intrinsically disordered proteins in E. coli
Download2015-01-01
Zahran, Somaya, Pan, Jonathan S., Liu, Philip B., Hwang, Peter M.
Many proteins contain intrinsically disordered regions that are highly solvent-exposed and susceptible to post-translational modifications. Studying these protein segments is critical to understanding their physiologic regulation, but proteolytic degradation can make them difficult to express and...
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Structure and proteolytic digestion of the intrinsically disordered C-terminal tail of cardiac troponin I
DownloadSpring 2019
Intrinsically disordered regions (IDRs) are protein sequences that do not acquire a fixed 3-D configuration under physiologic conditions. Their solvent-exposed nature makes them susceptible to post-translational modifications like proteolysis, which makes them vital for cellular regulation....
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Structure and proteolytic susceptibility of the inhibitory C-terminal tail of cardiac troponin I
Download2019-01-01
Mahmud, Zabed, Zahran, Somaya, Liu, Philip B., Reiz, Bela, Chan, Brandon Y.H., Roczkowsky, Andrej, McCartney, Christian-Scott E., Davies, Peter L., Li, Liang, Schulz, Richard, Hwang, Peter M.
Background Cardiac troponin I (cTnI) has two flexible tails that control the cardiac cycle. The C-terminal tail, cTnI135-209, binds actin to shut off cardiac muscle contraction, whereas the competing calcium-dependent binding of the switch region, cTnI146-158, by cardiac troponin C (cTnC)...