[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...
[NMR paper] Mechanisms of amyloid formation revealed by solution NMR.
Mechanisms of amyloid formation revealed by solution NMR.
Related Articles Mechanisms of amyloid formation revealed by solution NMR.
Prog Nucl Magn Reson Spectrosc. 2015 Aug;88-89:86-104
Authors: Karamanos TK, Kalverda AP, Thompson GS, Radford SE
Abstract
Amyloid fibrils are proteinaceous elongated aggregates involved in more than fifty human diseases. Recent advances in electron microscopy and solid state NMR have allowed the characterization of fibril structures to different extents of refinement. However, structural details...
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Mechanisms of amyloid formation revealed by solution NMR
Mechanisms of amyloid formation revealed by solution NMR
Publication date: Available online 26 May 2015
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Theodoros K. Karamanos , Arnout P. Kalverda , Gary S. Thompson , Sheena E. Radford</br>
Amyloid fibrils are proteinaceous elongated aggregates involved in more than fifty human diseases. Recent advances in electron microscopy and solid state NMR have allowed the characterization of fibril structures to different extents of refinement. However, structural details about the mechanism of...
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05-28-2015 12:56 AM
[NMR paper] Solution NMR assignment of the heavy chain complex of the human cardiac myosin regulatory light chain.
Solution NMR assignment of the heavy chain complex of the human cardiac myosin regulatory light chain.
Related Articles Solution NMR assignment of the heavy chain complex of the human cardiac myosin regulatory light chain.
Biomol NMR Assign. 2014 Jan 12;
Authors: Rostkova E, Gautel M, Pfuhl M
Abstract
The regulatory light chain (RLC) of striated and cardiac muscle myosin plays a complex role in muscle function and regulation. Together with the essential light chain it provides stability to the lever arm, which is essential for force...
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[NMR paper] Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils.
Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils.
Related Articles Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils.
Annu Rev Biophys. 2013 Mar 22;
Authors: Comellas G, Rienstra CM
Abstract
Protein structure determination methods using magic-angle spinning solidstate nuclear magnetic resonance (MAS SSNMR) have experienced a remarkable...
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[NMR paper] Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain.
Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain.
Biomol NMR Assign. 2013 Jan 22;
Authors: Orbán-Németh Z, Henen MA, Geist L, Zerko S, Saxena S, Stanek J, Ko?mi?ski W, Propst F, Konrat R
Abstract
Microtubule-associated protein 1B (MAP1B) is a classical...
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[NMR paper] Conformational differences between complexes of elongation factor Tu studied 19F-NMR
Conformational differences between complexes of elongation factor Tu studied 19F-NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Conformational differences between complexes of elongation factor Tu studied 19F-NMR spectroscopy.
Eur J Biochem. 1993 Dec 15;218(3):1041-7
Authors: Eccleston JF, Molloy DP, Hinds MG, King RW, Feeney J
An analogue of elongation factor Tu (EF-Tu) from Escherichia coli was prepared by...
Differences in Protein Concentration Dependence forNucleation and Elongation in Light Chain Amyloid Formation
Linear Mode
