Natronomonas pharaonis halorhodopsin (NpHR) is a light-driven Cl^(-) inward pump that is widely used as an optogenetic tool. Although NpHR is previously extensively studied, its Cl^(-) uptake process is not well understood from the protein structure perspective, mainly because in crystalline lattice, it has been difficult to analyze the structural changes associated with the Cl^(-) uptake process. In this study, we used solid-state NMR to analyze NpHR both in the Cl^(-)-bound and -free states...
[NMR paper] Structural details of amyloid beta oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopy
Structural details of amyloid beta oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopy
Human PrP (huPrP) is a high-affinity receptor for oligomeric amyloid-? (A?) protein aggregates. Binding of A? oligomers to membrane-anchored huPrP has been suggested to trigger neurotoxic cell signaling in Alzheimer's disease, while an N-terminal soluble fragment of huPrP can sequester A? oligomers and reduce their toxicity. Synthetic oligomeric A? species are known to be heterogeneous, dynamic and transient, rendering their structural investigation particularly...
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[NMR paper] Photocycle-dependent conformational changes in the proteorhodopsin cross-protomer Asp-His-Trp triad revealed by DNP-enhanced MAS-NMR.
Photocycle-dependent conformational changes in the proteorhodopsin cross-protomer Asp-His-Trp triad revealed by DNP-enhanced MAS-NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full_free.gif http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.png Related Articles Photocycle-dependent conformational changes in the proteorhodopsin cross-protomer Asp-His-Trp triad revealed by DNP-enhanced MAS-NMR.
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[NMR paper] Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy.
Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy.
Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy.
Nat Commun. 2017 Sep 29;8(1):753
Authors: Theint T, Nadaud PS, Aucoin D, Helmus JJ, Pondaven SP, Surewicz K, Surewicz WK, Jaroniec CP
Abstract
One of the most puzzling aspects of the prion diseases is the intricate relationship between prion strains and interspecies transmissibility barriers....
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10-01-2017 09:32 PM
Structural Changes Associated with Transthyretin Misfoldingand Amyloid Formation Revealed by Solution and Solid-State NMR
Structural Changes Associated with Transthyretin Misfoldingand Amyloid Formation Revealed by Solution and Solid-State NMR
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00164/20160323/images/medium/bi-2016-00164v_0004.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00164
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[NMR paper] Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.
Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.
Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.
Biochemistry. 2016 Mar 21;
Authors: Lim KH, Dasari AK, Hung I, Gan Z, Kelly JW, Wemmer DE
Abstract
Elucidation of structural changes involved in protein misfolding and amyloid formation is crucial for unraveling the molecular basis of amyloid formation. Here we report structural...
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[NMR paper] Nutrient-dependent structural changes in S. aureus peptidoglycan revealed by solid-state NMR spectroscopy.
Nutrient-dependent structural changes in S. aureus peptidoglycan revealed by solid-state NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Nutrient-dependent structural changes in S. aureus peptidoglycan revealed by solid-state NMR spectroscopy.
Biochemistry. 2012 Oct 16;51(41):8143-53
Authors: Zhou X, Cegelski L
Abstract
The bacterial cell wall is essential to cell survival and is a major target of antibiotics. The main component of the...
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04-02-2013 07:23 PM
[NMR paper] Early and late M intermediates in the bacteriorhodopsin photocycle: a solid-state NMR
Early and late M intermediates in the bacteriorhodopsin photocycle: a solid-state NMR study.
Related Articles Early and late M intermediates in the bacteriorhodopsin photocycle: a solid-state NMR study.
Biochemistry. 1998 Jun 2;37(22):8088-96
Authors: Hu JG, Sun BQ, Bizounok M, Hatcher ME, Lansing JC, Raap J, Verdegem PJ, Lugtenburg J, Griffin RG, Herzfeld J
To enforce vectorial proton transport in bacteriorhodopsin (bR), it is necessary that there be a change in molecular structure between deprotonation and reprotonation of the...
Structural changes of Natronomonas pharaonis halorhodopsin in its late photocycle revealed by solid-state NMR spectroscopy
Linear Mode
