[NMR paper] Protein-Solvent Interfaces in Human Y145Stop Prion Protein Amyloid Fibrils Probed by Paramagnetic Solid-State NMR Spectroscopy.
Protein-Solvent Interfaces in Human Y145Stop Prion Protein Amyloid Fibrils Probed by Paramagnetic Solid-State NMR Spectroscopy.
Related Articles Protein-Solvent Interfaces in Human Y145Stop Prion Protein Amyloid Fibrils Probed by Paramagnetic Solid-State NMR Spectroscopy.
J Struct Biol. 2018 Apr 18;:
Authors: Aucoin D, Xia Y, Theint T, Nadaud PS, Surewicz K, Surewicz WK, Jaroniec CP
Abstract
The C-terminally truncated Y145Stop variant of prion protein (PrP23-144), which is associated with heritable PrP cerebral amyloid angiopathy...
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04-22-2018 10:46 PM
Protein-Solvent Interfaces in Human Y145Stop Prion Protein Amyloid Fibrils Probed by Paramagnetic Solid-State NMR Spectroscopy
Protein-Solvent Interfaces in Human Y145Stop Prion Protein Amyloid Fibrils Probed by Paramagnetic Solid-State NMR Spectroscopy
Publication date: Available online 18 April 2018
Source:Journal of Structural Biology</br>
Author(s): Darryl Aucoin, Yongjie Xia, Theint Theint, Philippe S. Nadaud, Krystyna Surewicz, Witold K. Surewicz, Christopher P. Jaroniec</br>
The C-terminally truncated Y145Stop variant of prion protein (PrP23-144), which is associated with heritable PrP cerebral amyloid angiopathy in humans and also capable of triggering a transmissible...
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04-18-2018 01:41 PM
[NMR paper] Probing the Atomic Structure of Transient Protein Contacts by Paramagnetic Relaxation Enhancement Solution NMR.
Probing the Atomic Structure of Transient Protein Contacts by Paramagnetic Relaxation Enhancement Solution NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Probing the Atomic Structure of Transient Protein Contacts by Paramagnetic Relaxation Enhancement Solution NMR.
Methods Mol Biol. 2018;1688:243-255
Authors: Venditti V, Fawzi NL
Abstract
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11-21-2017 10:10 PM
Characterization of Protein–Protein Interfaces in Large Complexes by Solid-State NMR Solvent Paramagnetic Relaxation Enhancements
Characterization of Protein–Protein Interfaces in Large Complexes by Solid-State NMR Solvent Paramagnetic Relaxation Enhancements
Carl O?ster, Simone Kosol, Christoph Hartlmu?ller, Jonathan M. Lamley, Dinu Iuga, Andres Oss, Mai-Liis Org, Kalju Vanatalu, Ago Samoson, Tobias Madl and Jo?zef R. Lewandowski
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.7b03875/20170824/images/medium/ja-2017-038753_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.7b03875
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA ...
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08-25-2017 05:31 PM
[NMR paper] Characterization of protein-protein interfaces in large complexes by solid state NMR solvent paramagnetic relaxation enhancements.
Characterization of protein-protein interfaces in large complexes by solid state NMR solvent paramagnetic relaxation enhancements.
Related Articles Characterization of protein-protein interfaces in large complexes by solid state NMR solvent paramagnetic relaxation enhancements.
J Am Chem Soc. 2017 Aug 07;:
Authors: Öster C, Kosol S, Hartlmüller C, Lamley JM, Iuga D, Oss A, Org ML, Vanatalu K, Samoson A, Madl T, Lewandowski JR
Abstract
Solid-state NMR is becoming a viable alternative for obtaining information about structures and...
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08-07-2017 07:31 PM
Requirements on Paramagnetic Relaxation Enhancement Data for Membrane Protein Structure Determination by NMR
Requirements on Paramagnetic Relaxation Enhancement Data for Membrane Protein Structure Determination by NMR
6 June 2012
Publication year: 2012
Source:Structure, Volume 20, Issue 6</br>
</br>
Nuclear magnetic resonance (NMR) structure calculations of the ?-helical integral membrane proteins DsbB, GlpG, and halorhodopsin show that distance restraints from paramagnetic relaxation enhancement (PRE) can provide sufficient structural information to determine their structure with an accuracy of about 1.5*Å in the absence of other long-range conformational restraints. Our...
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02-03-2013 10:13 AM
Solid-State NMR of a Large Membrane Protein by Paramagnetic Relaxation Enhancement.
Solid-State NMR of a Large Membrane Protein by Paramagnetic Relaxation Enhancement.
Solid-State NMR of a Large Membrane Protein by Paramagnetic Relaxation Enhancement.
J Phys Chem Lett. 2011 Jul 21;2(14):1836-1841
Authors: Tang M, Berthold DA, Rienstra CM
Membrane proteins play an important role in many biological functions. Solid-state NMR spectroscopy is uniquely suited for studying structure and dynamics of membrane proteins in a membranous environment. The major challenge to obtain high quality solid-state NMR spectra of membrane proteins is...
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08-16-2011 01:19 PM
[Question from NMRWiki Q&A forum] Relaxation editing vr paramagnetic relaxation enhancement experiments - 13C CP-MAS NM
Relaxation editing vr paramagnetic relaxation enhancement experiments - 13C CP-MAS NMR
I am a beginner in NMR spectroscopy and I would like to learn more about relaxation editing experiments vs PRE. A colleague of mine is doing the 13C CP-MAS NMR experim. and he using cellulose II powder, regenerated cellulose and milled reg cellulose. We are interested in C4 resonance of cellulose II, good resolved resonance, to better understand the supramolecular structure of cellulose II. As experiments: long relaxation experiments - PRE with aqueous CuSO4 solution of certain concentration, does the...
Atomic view of cosolute-induced protein denaturation probed by NMR solvent paramagnetic relaxation enhancement - pnas.org
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