The DegP protease-chaperone operates within the periplasm of Gram-negative bacteria, where it assists in the regulation of protein homeostasis, promotes virulence, and is essential to survival under stress. To carry out these tasks, DegP forms a network of preorganized apo oligomers that facilitate the capture of substrates within distributions of cage-like complexes which expand to encapsulate clients of various sizes. Although the architectures of DegP cage complexes are well understood,...
[NMR paper] NMR lineshape analysis*using analytical solutions of multi-state chemical exchange with applications to kinetics of host-guest systems
NMR lineshape analysis*using analytical solutions of multi-state chemical exchange with applications to kinetics of host-guest systems
Nuclear magnetic resonance (NMR) lineshape analysis is a powerful tool for the study of chemical kinetics. Here we provide techniques for analysis of the relationship between experimentally observed spin kinetics (transitions between different environments ) and corresponding chemical kinetics (transitions between distinct chemical species; e.g., free host and complexed host molecule). The advantages of using analytical solutions for two-, three- or...
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10-19-2022 03:14 AM
An allosteric switch regulates Mycobacterium tuberculosis ClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR [Biophysics and Computational Biology]
An allosteric switch regulates Mycobacterium tuberculosis ClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR
Siavash Vahidi, Zev A. Ripstein, Jordan B. Juravsky, Enrico Rennella, Alfred L. Goldberg, Anthony K. Mittermaier, John L. Rubinstein, Lewis E. Kay...
Date: 2020-03-17
The 300-kDa ClpP1P2 protease from Mycobacterium tuberculosis collaborates with the AAA+ (ATPases associated with a variety of cellular activities) unfoldases, ClpC1 and ClpX, to degrade substrate proteins. Unlike in other bacteria, all of the components of the Clp system are essential for...
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03-18-2020 10:42 AM
Exploring long-range cooperativity in the 20S proteasome core particle from Thermoplasma acidophilum using methyl-TROSY-based NMR [Biophysics and Computational Biology]
Exploring long-range cooperativity in the 20S proteasome core particle from Thermoplasma acidophilum using methyl-TROSY-based NMR
Enrico Rennella, Rui Huang, Zanlin Yu, Lewis E. Kay...
Date: 2020-03-10
The 20S core particle (CP) proteasome is a molecular assembly catalyzing the degradation of misfolded proteins or proteins no longer required for function. It is composed of four stacked heptameric rings that form a barrel-like structure, sequestering proteolytic sites inside its lumen. Proteasome function is regulated by gates derived from... Read More
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Number: 10
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03-16-2020 04:59 PM
[NMR paper] An allosteric switch regulates Mycobacterium tuberculosis ClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR.
An allosteric switch regulates Mycobacterium tuberculosis ClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR.
Related Articles An allosteric switch regulates Mycobacterium tuberculosis ClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR.
Proc Natl Acad Sci U S A. 2020 Mar 02;:
Authors: Vahidi S, Ripstein ZA, Juravsky JB, Rennella E, Goldberg AL, Mittermaier AK, Rubinstein JL, Kay LE
Abstract
The 300-kDa ClpP1P2 protease from Mycobacterium tuberculosis collaborates with the AAA+ (ATPases...
Host-Guest Complexes as Water-Soluble High-Performance DNP Polarizing Agents
From The DNP-NMR Blog:
Host-Guest Complexes as Water-Soluble High-Performance DNP Polarizing Agents
Mao, J., et al., Host-Guest Complexes as Water-Soluble High-Performance DNP Polarizing Agents. J Am Chem Soc, 2013. 135(51): p. 19275-81.
http://www.ncbi.nlm.nih.gov/pubmed/24279469
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01-10-2014 06:01 PM
Chemistry and Structureof a Host–Guest Relationship:The Power of NMR and X-ray Diffraction in Tandem
Chemistry and Structureof a Host–Guest Relationship:The Power of NMR and X-ray Diffraction in Tandem
Qi-Qiang Wang, Victor W. Day and Kristin Bowman-James
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja3096762/aop/images/medium/ja-2012-096762_0013.gif
Journal of the American Chemical Society
DOI: 10.1021/ja3096762
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/Ze2zN3_VFiU
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12-20-2012 04:48 PM
1H NMR Chemical Shift Calculations as a Probe of Supramolecular Host–Guest Geometry
1H NMR Chemical Shift Calculations as a Probe of Supramolecular Host–Guest Geometry
Jeffrey S. Mugridge, Robert G. Bergman and Kenneth N. Raymond
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja202254x/aop/images/medium/ja-2011-02254x_0010.gif
Journal of the American Chemical Society
DOI: 10.1021/ja202254x
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/wR-1b5WtJhc
Exploring Host-Guest Interactions within a 600 kDa DegP Protease Cage Complex Using Hydrodynamics Measurements and Methyl-TROSY NMR
Linear Mode
