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Skip to Search Results- 4Intrinsically disordered regions
- 3Chemical cleavage
- 3Fusion protein expression
- 2Escherichia coli
- 2Inclusion bodies
- 2Nickel ion-catalyzed peptide bond hydrolysis
- 2Medicine, Department of
- 2Medicine, Department of/General Internal Medicine
- 1Graduate and Postdoctoral Studies (GPS), Faculty of
- 1Graduate and Postdoctoral Studies (GPS), Faculty of/Theses and Dissertations
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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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Recombinant expression of the cardiac troponin I fragment, cTnI[135-209], that controls cardiac contraction
Download2015-05-14
Jonathan S. Pan, Somaya Zahran, Peter M Hwang
Intrinsically disordered regions (IDRs) are protein segments that lack a fixed three-dimensional structure under physiologic conditions, they are susceptible to post-translational modifications such as proteolysis. However, they are highly important in cellular signal transduction and the...
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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....