Wide-line šH NMR is an efficient spectroscopic method to determine the disorder tendency of a protein. It directly measures the properties of the hydration shell of proteins, delivering exact and measurable values of their disorder/order content. A comparison is performed between several globular and disordered proteins. The common properties of the subzero mobile hydration water of these two groups were investigated. The amount of the mobile hydration water and the shape of the melting diagram...
[NMR paper] Wide-Line NMR Melting Diagrams, Their Thermodynamic Interpretation, and Secondary Structure Predictions for A30P and E46K ?-Synuclein
Wide-Line NMR Melting Diagrams, Their Thermodynamic Interpretation, and Secondary Structure Predictions for A30P and E46K ?-Synuclein
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...
nmrlearner
Journal club
0
06-13-2022 11:54 AM
[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...
...
nmrlearner
Journal club
0
06-02-2021 05:10 PM
The PROSECCO server for chemical shift predictions in ordered and disordered proteins
The PROSECCO server for chemical shift predictions in ordered and disordered proteins
Abstract
The chemical shifts measured in solution-state and solid-state nuclear magnetic resonance (NMR) are powerful probes of the structure and dynamics of protein molecules. The exploitation of chemical shifts requires methods to correlate these data with the protein structures and sequences. We present here an approach to calculate accurate chemical shifts in both ordered and disordered proteins using exclusively the information contained in their sequences....
nmrlearner
Journal club
0
11-09-2017 08:55 AM
[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...
nmrlearner
Journal club
0
07-16-2016 10:22 PM
[NMR paper] NMR Methods for the Study of Instrinsically Disordered Proteins Structure, Dynamics, and Interactions: General Overview and Practical Guidelines.
NMR Methods for the Study of Instrinsically Disordered Proteins Structure, Dynamics, and Interactions: General Overview and Practical Guidelines.
Related Articles NMR Methods for the Study of Instrinsically Disordered Proteins Structure, Dynamics, and Interactions: General Overview and Practical Guidelines.
Adv Exp Med Biol. 2015;870:49-122
Authors: Brutscher B, Felli IC, Gil-Caballero S, Hoek T, Kümmerle R, Piai A, Pierattelli R, Sólyom Z
Abstract
Thanks to recent improvements in NMR instrumentation, pulse sequence design, and...
nmrlearner
Journal club
0
09-21-2015 03:01 PM
[NMR paper] Longitudinal relaxation properties of (1)H(N) and (1)H(?) determined by direct-detected (13)C NMR experiments to study intrinsically disordered proteins (IDPs).
Longitudinal relaxation properties of (1)H(N) and (1)H(?) determined by direct-detected (13)C NMR experiments to study intrinsically disordered proteins (IDPs).
Longitudinal relaxation properties of (1)H(N) and (1)H(?) determined by direct-detected (13)C NMR experiments to study intrinsically disordered proteins (IDPs).
J Magn Reson. 2015 Feb 12;254:19-26
Authors: Hoek T, Gil-Caballero S, Pierattelli R, Brutscher B, Felli IC
Abstract
Intrinsically disordered proteins (IDPs) are functional proteins containing large...
nmrlearner
Journal club
0
03-17-2015 05:12 PM
Longitudinal relaxation properties of 1HN and 1H? determined by direct-detected 13C NMR experiments to study intrinsically disordered proteins (IDPs)
Longitudinal relaxation properties of 1HN and 1H? determined by direct-detected 13C NMR experiments to study intrinsically disordered proteins (IDPs)
Publication date: Available online 12 February 2015
Source:Journal of Magnetic Resonance</br>
Author(s): Tomá Hoek , Sergi Gil-Caballero , Roberta Pierattelli , Bernhard Brutscher , Isabella C. Felli</br>
Intrinsically disordered proteins (IDPs) are functional proteins containing large fragments characterized by high local mobility. Bioinformatic studies have suggested that a significant fraction (more than 30%)...
General Characterization of Properties of Ordered and Disordered Proteins by Wide-Line (1)H NMR
Linear Mode
