The cosolvent effect arises from the interaction of cosolute molecules with a protein and alters the equilibrium between native and unfolded states. Denaturants shift the equilibrium toward the latter, while osmolytes stabilize the former. The molecular mechanism whereby cosolutes perturb protein stability is still the subject of considerable debate. Probing the molecular details of the cosolvent effect is experimentally challenging as the interactions are very weak and transient, rendering them...
Atomic view of cosolute-induced protein denaturation probed by NMR solvent paramagnetic relaxation enhancement [Chemistry]
Atomic view of cosolute-induced protein denaturation probed by NMR solvent paramagnetic relaxation enhancement
Yusuke Okuno, Janghyun Yoo, Charles D. Schwieters, Robert B. Best, Hoi Sung Chung, G. Marius Clore...
Date: 2021-08-17
The cosolvent effect arises from the interaction of cosolute molecules with a protein and alters the equilibrium between native and unfolded states. Denaturants shift the equilibrium toward the latter, while osmolytes stabilize the former. The molecular mechanism whereby cosolutes perturb protein stability is still the subject of considerable debate....
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08-18-2021 11:11 AM
[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
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...
Atomic view of cosolute-induced protein denaturation probed by NMR solvent paramagnetic relaxation enhancement
Linear Mode
