Parkinson's disease is thought to be caused by aggregation of the intrinsically disordered protein, ?-synuclein. Two amyloidogenic variants, A30P, and E46K familial mutants were investigated by wide-line šH NMR spectrometry as a completion of our earlier work on wild-type and A53T ?-synuclein (Bokor M. et al. WT and A53T ?-synuclein systems: melting diagram and its new interpretation. Int. J. Mol. Sci.2020, 21, 3997.). A monolayer of mobile water molecules hydrates A30P ?-synuclein at the lowest...
[NMR paper] Protein-Protein Connections-Oligomer, Amyloid and Protein Complex-By Wide Line (1)H NMR
Protein-Protein Connections-Oligomer, Amyloid and Protein Complex-By Wide Line (1)H NMR
The amount of bonds between constituting parts of a protein aggregate were determined in wild type (WT) and A53T ?-synuclein (?S) oligomers, amyloids and in the complex of thymosin-?(4)-cytoplasmic domain of stabilin-2 (T?(4)-stabilin CTD). A53T ?S aggregates have more extensive ?sheet contents reflected by constant regions at low potential barriers in difference (to monomers) melting diagrams (MDs). Energies of the intermolecular interactions and of secondary structures bonds, formed during...
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06-02-2021 05:10 PM
[NMR paper] Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment.
Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment.
Related Articles Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment.
BMB Rep. 2016 Apr 4;
Authors: Tompa P, Kim KH, Bokor M, Kamasa P, Tantos Á, Fritz B, Kim DH, Lee C, Verebélyi T, Tompa K
Abstract
Wide-line 1H NMR intensity and differential scanning calorimetry measurements were carried out on the intrinsically disordered...
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07-16-2016 10:22 PM
[NMR paper] CSI 3.0: a web server for identifying secondary and super-secondary structure in proteins using NMR chemical shifts.
CSI 3.0: a web server for identifying secondary and super-secondary structure in proteins using NMR chemical shifts.
Related Articles CSI 3.0: a web server for identifying secondary and super-secondary structure in proteins using NMR chemical shifts.
Nucleic Acids Res. 2015 May 15;
Authors: Hafsa NE, Arndt D, Wishart DS
Abstract
The Chemical Shift Index or CSI 3.0 (http://csi3.wishartlab.com) is a web server designed to accurately identify the location of secondary and super-secondary structures in protein chains using only...
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05-17-2015 03:52 PM
[NMR paper] In-Cell NMR Characterization of the Secondary Structure Populations of a Disordered Conformation of ?-Synuclein within E. coli Cells.
In-Cell NMR Characterization of the Secondary Structure Populations of a Disordered Conformation of ?-Synuclein within E. coli Cells.
In-Cell NMR Characterization of the Secondary Structure Populations of a Disordered Conformation of ?-Synuclein within E. coli Cells.
PLoS One. 2013;8(8):e72286
Authors: Waudby CA, Camilloni C, Fitzpatrick AW, Cabrita LD, Dobson CM, Vendruscolo M, Christodoulou J
Abstract
?-Synuclein is a small protein strongly implicated in the pathogenesis of Parkinson's disease and related neurodegenerative disorders. We...
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08-31-2013 06:56 PM
[NMR paper] A molecular dynamics simulations-based interpretation of NMR multidimensional heteronuclear spectra of alpha-synuclein/dopamine adducts.
A molecular dynamics simulations-based interpretation of NMR multidimensional heteronuclear spectra of alpha-synuclein/dopamine adducts.
Related Articles A molecular dynamics simulations-based interpretation of NMR multidimensional heteronuclear spectra of alpha-synuclein/dopamine adducts.
Biochemistry. 2013 Aug 21;
Authors: Dibenedetto D, Rossetti G, Caliandro R, Carloni P
Abstract
Multidimensional heteronuclear NMR spectroscopy provides valuable structural information on adducts between naturally unfolded proteins and their ligands....
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08-24-2013 04:53 PM
[NMR paper] Thermodynamic and solution state NMR characterization of the binding of secondary and conjugated bile acids to STARD5.
Thermodynamic and solution state NMR characterization of the binding of secondary and conjugated bile acids to STARD5.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Thermodynamic and solution state NMR characterization of the binding of secondary and conjugated bile acids to STARD5.
Biochim Biophys Acta. 2013 Jul 16;
Authors: Létourneau D, Lorin A, Lefebvre A, Cabana J, Lavigne P, Lehoux JG
Abstract
STARD5 is a member of the STARD4 sub-family...
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07-23-2013 09:52 PM
[NMR images] The basis of NMR spectroscopy, PPT PowerPoint drawing diagrams ...
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The basis of NMR spectroscopy, PPT PowerPoint drawing diagrams ...
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06-27-2013 02:10 PM
[NMR paper] Thermodynamic interpretation of protein dynamics from NMR relaxation measurements.
Thermodynamic interpretation of protein dynamics from NMR relaxation measurements.
Related Articles Thermodynamic interpretation of protein dynamics from NMR relaxation measurements.
Protein Pept Lett. 2005 Apr;12(3):235-40
Authors: Spyracopoulos L
Protein dynamics and thermodynamics can be characterized through measurements of relaxation rates of side chain (2)H and (13)C, and backbone (15)N nuclei using NMR spectroscopy. The rates reflect protein motions on timescales from picoseconds to milliseconds. Backbone and methyl side chain NMR...
Wide-Line NMR Melting Diagrams, Their Thermodynamic Interpretation, and Secondary Structure Predictions for A30P and E46K ?-Synuclein
Linear Mode
