[NMR paper] Roles of structural plasticity in chaperone HdeA activity are revealed by 19F NMR.
Roles of structural plasticity in chaperone HdeA activity are revealed by 19F NMR.
Related Articles Roles of structural plasticity in chaperone HdeA activity are revealed by 19F NMR.
Chem Sci. 2016 Mar 01;7(3):2222-2228
Authors: Zhai Z, Wu Q, Zheng W, Liu M, Pielak GJ, Li C
Abstract
HdeA, a minimal ATP-independent acid chaperone, is crucial for the survival of enteric pathogens as they transit the acidic (pH 1-3) environment of the stomach. Although protein disorder (unfolding) and structural plasticity have been elegantly linked...
nmrlearner
Journal club
0
06-20-2018 08:56 PM
[NMR paper] Enzyme responsive LipoCEST agents: assessment of MMP-2 activity by measuring the intra-liposomal water 1H-NMR resonance shift.
Enzyme responsive LipoCEST agents: assessment of MMP-2 activity by measuring the intra-liposomal water 1H-NMR resonance shift.
Related Articles Enzyme responsive LipoCEST agents: assessment of MMP-2 activity by measuring the intra-liposomal water 1H-NMR resonance shift.
Angew Chem Int Ed Engl. 2017 Jul 26;:
Authors: Ferrauto G, Di Gregorio E, Ruzza M, Catanzaro V, Padovan S, Aime S
Abstract
Mobile proton containing solutes can be detected by MRI via Chemical Exchange Saturation Transfer(CEST)method. The CEST sensitivity is...
nmrlearner
Journal club
0
07-27-2017 04:37 PM
[NMR paper] Enzyme responsive LipoCEST agents: assessment of MMP-2 activity by measuring the intra-liposomal water 1H-NMR resonance shift
Enzyme responsive LipoCEST agents: assessment of MMP-2 activity by measuring the intra-liposomal water 1H-NMR resonance shift
Mobile proton containing solutes can be detected by MRI via Chemical Exchange Saturation Transfer(CEST)method. The CEST sensitivity is dramatically enhanced by using, as exchanging protons, the water molecules confined inside liposomes, properly shifted by a paramagnetic Shift Reagent. The chemical shift of the intraliposomal water resonance(?IL) is affected by the overall shape of the supramolecular system. Herein, it is shown that ?IL of a spherical LipoCEST...
nmrlearner
Journal club
0
07-27-2017 01:04 AM
[NMR paper] Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation.
Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation.
Related Articles Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation.
Proc Natl Acad Sci U S A. 2016 Jun 13;
Authors: Shu Q, Krezel AM, Cusumano ZT, Pinkner JS, Klein R, Hultgren SJ, Frieden C
Abstract
Curli, consisting primarily of major structural subunit CsgA, are functional amyloids produced on the surface of...
nmrlearner
Journal club
0
06-15-2016 11:12 PM
Cytoplasmic Heme-Binding Protein (HutX) from Vibrio cholerae Is an Intracellular Heme Transport Proteinfor the Heme-Degrading Enzyme, HutZ
Cytoplasmic Heme-Binding Protein (HutX) from Vibrio cholerae Is an Intracellular Heme Transport Proteinfor the Heme-Degrading Enzyme, HutZ
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01273/20160203/images/medium/bi-2015-01273d_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01273
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/TZY3CBAo0xw
More...
Toward Quantitative Measurements of Enzyme Kinetics by Dissolution Dynamic Nuclear Polarization
From The DNP-NMR Blog:
Toward Quantitative Measurements of Enzyme Kinetics by Dissolution Dynamic Nuclear Polarization
Miclet E, Abergel D, Bornet A, Milani J, Jannin S, Bodenhausen G. Toward Quantitative Measurements of Enzyme Kinetics by Dissolution Dynamic Nuclear Polarization. The Journal of Physical Chemistry Letters. 2014;5(19):3290-5.
http://dx.doi.org/10.1021/jz501411d
nmrlearner
News from NMR blogs
0
06-03-2015 11:04 PM
[NMR paper] Relation of enzyme activity to local/global stability of murine adenosine deaminase:
Relation of enzyme activity to local/global stability of murine adenosine deaminase: 19F NMR studies.
Related Articles Relation of enzyme activity to local/global stability of murine adenosine deaminase: 19F NMR studies.
J Mol Biol. 2005 Jan 21;345(3):599-610
Authors: Shu Q, Frieden C
Adenosine deaminase (ADA, EC 3.5.4.4) is a ubiquitous (beta/alpha)8-barrel enzyme crucial for purine metabolism and normal immune competence. In this study, it was observed that loss of enzyme activity of murine ADA (mADA) precedes the global secondary and...