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A PagP fusion protein system for the expression of intrinsically disordered proteins in E. coli
Download2012-01-01
Hwang, Peter M., Pan, Jonathan S., Sykes, Brian D.
PagP, a beta-barrel membrane protein found in Gram-negative bacteria, expresses robustly in inclusion bodies when its signal sequence is removed. We have developed a new fusion protein expression system based on PagP and demonstrated its utility in the expression of the unstructured N-terminal...
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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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Exploiting bacterial glycosylation machineries for the synthesis of a Lewis antigen-containing glycoprotein
Download2011
Hug, Isabelle, Reiz, Bela, Fentabil, Messele A., Klassen, John S., Whittal, Randy M., Zheng, Blake, Feldman, Mario F.
Glycoproteins constitute a class of compounds of increasing importance for pharmaceutical applications. The manipulation of bacterial protein glycosylation systems from Gram-negative bacteria for the synthesis of recombinant glycoproteins is a promising alternative to the current production...
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Stereo-selective deuteration in aspartate, asparagine, lysine, and methionine amino acid residues using fumarate as a carbon source for E. coli in D2O
Download2017-01-01
Danmaliki, Gaddafi I., Liu, Philip B., Hwang, Peter M.
We propose an isotope labeling strategy for expressing proteins in E. coli using protonated natural abundance 12C carbon sources in D2O. The strategy eliminates dominant 1H-13C and 1H-1H dipolar relaxation mechanisms to produce long-lived magnetization for solution NMR spectroscopy. Isolated 1H...
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Structure and Function of Cardiac Troponin C (TNNC1): Implications for Heart Failure, Cardiomyopathies, and Troponin Modulating Drugs
Download2015-01-01
Li, Monica X., Hwang, Peter M.
In striated muscle, the protein troponin complex turns contraction on and off in a calcium-dependent manner. The calcium-sensing component of the complex is troponin C, which is expressed from the TNNC1 gene in both cardiac muscle and slow-twitch skeletal muscle (identical transcript in both...
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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)...
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2016-01-01
Cai, Fangze, Li, Monica X., Pineda-Sanbria, Sandra E., Gelozia, Shorena, Lindert, Steffen, West, Frederick, Sykes, Brian D., Hwang, Peter M.
In cardiac and skeletal muscle, the troponin complex turns muscle contraction on and off in a calcium-dependent manner. Many small molecules are known to bind to the troponin complex to modulate its calcium binding affinity, and this may be useful in a broad range of conditions in which striated...