TABLE OF CONTENTS |
April 2017 Volume 13, Issue 4 |
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| Commentary Research Highlights News and Views Review Brief Communications Articles
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Commentary | Top |
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Simultaneous quantification of protein order and disorder pp339 - 342 Pietro Sormanni, Damiano Piovesan, Gabriella T Heller, Massimiliano Bonomi, Predrag Kukic et al. doi:10.1038/nchembio.2331 Nuclear magnetic resonance spectroscopy is transforming our views of proteins by revealing how their structures and dynamics are closely intertwined to underlie their functions and interactions. Compelling representations of proteins as statistical ensembles are uncovering the presence and biological relevance of conformationally heterogeneous states, thus gradually making it possible to go beyond the dichotomy between order and disorder through more quantitative descriptions that span the continuum between them.
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Research Highlights | Top |
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Development: Marking the transition | Bioconjugation: Methionine's time to shine | Drug discovery: Uncoupling coupled transport | Imaging: Luciferase matchmaker
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News and Views | Top |
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Review | Top |
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Versatile modes of cellular regulation via cyclic dinucleotides pp350 - 359 Petya Violinova Krasteva and Holger Sondermann doi:10.1038/nchembio.2337 A review of the roles of cyclic dinucleotides (CDNs) in signaling systems including transcription, ion transport, bacterial secretion and eukaryotic immune responses, highlighting the diverse binding modes of CDNs by target proteins and functional insights gained from structural studies.
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Brief Communications | Top |
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Ligand-promoted protein folding by biased kinetic partitioning pp369 - 371 Karan S Hingorani, Matthew C Metcalf, Derrick T Deming, Scott C Garman, Evan T Powers et al. doi:10.1038/nchembio.2303
Pharmacological chaperones improve folding of destabilized Escherichia coli dihydrofolate reductase (DHFR) and human disease-linked α-galactosidase A (α-GAL) by biasing the kinetic partitioning between folding, aggregation, and degradation. Chaperoning spares DHFR from aggregation and α-GAL from degradation.
See also: News and Views by Hatters
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Articles | Top |
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A water-mediated allosteric network governs activation of Aurora kinase A pp402 - 408 Soreen Cyphers, Emily F Ruff, Julie M Behr, John D Chodera and Nicholas M Levinson doi:10.1038/nchembio.2296
Spectroscopic studies of allosteric activation of Aurora A kinase using a site-specific infrared probe combined with FRET analysis and molecular dynamics simulations reveals a water-mediated hydrogen bond network in the active site that regulates Aurora A activity.
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A tight tunable range for Ni(II) sensing and buffering in cells pp409 - 414 Andrew W Foster, Rafael Pernil, Carl J Patterson, Andrew J P Scott, Lars-Olof Palsson et al. doi:10.1038/nchembio.2310
The Ni(ii) affinity of Ni(ii) sensor InrS is attuned to buffered Ni(ii) concentrations, explaining why these two parameters co-vary for different metals over many orders of magnitude.
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Evolution of a split RNA polymerase as a versatile biosensor platform pp432 - 438 Jinyue Pu, Julia Zinkus-Boltz and Bryan C Dickinson doi:10.1038/nchembio.2299
Design of a proximity-dependent split RNA polymerase system and its optimization by phage-assisted continuous evolution (PACE) enabled the development of a family of activity-dependent split RNA polymerase biosensors regulated by small molecules or light.
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The GlcN6P cofactor plays multiple catalytic roles in the glmS ribozyme pp439 - 445 Jamie L Bingaman, Sixue Zhang, David R Stevens, Neela H Yennawar, Sharon Hammes-Schiffer et al. doi:10.1038/nchembio.2300
Experimental work and computational modeling together reveal a suite of catalytic roles of the GlcN6P cofactor in the glmS ribozyme, including activation of the nucleophile, electrostatic stabilization, and alignment of the active site.
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