Common molecular pathogenesis of disease-related intrinsically disordered proteins revealed by NMR analysis.
J Biochem. 2017 Sep 11;:
Authors: Shigemitsu Y, Hiroaki H
Abstract
Intrinsically disordered proteins (IDPs) are either completely unstructured or contain large disordered regions in their native state; they have drawn much attention in the field of molecular pathology. Some of them substantially tend to form protein self-assemblies, such as toxic or non-toxic aggregates and fibrils, and have been postulated to relate to diseases. These disease-related IDPs include A?(1-42) [Alzheimer's disease (AD)], Tau (AD and tauopathy), ?-synuclein (Parkinson's disease), and p53 (cancer). Several studies suggest that these aggregation and/or fibril formation processes are often initiated by transient conformational changes of the IDPs prior to protein self-assembly. Interestingly, the pathological molecular processes of these IDPs share multiple common features with those of protein misfolding diseases, such as transmissible spongiform encephalopathy (PrPsc) and AL-amyloidosis (VL-domain of ?-immunoglobulin). This review provides an overview of solution NMR techniques that can help analyze the early and transient events of conformational equilibrium of IDPs and folded proteins.
PMID: 28992347 [PubMed - as supplied by publisher]
[NMR paper] Multi-Timescale Dynamics in Intrinsically Disordered Proteins from NMR Relaxation and Molecular Simulation.
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J Phys Chem Lett. 2016 Jun 14;
Authors: Salvi N, Abyzov A, Blackledge M
Abstract
Intrinsically disordered proteins (IDPs) access highly diverse ensembles of conformations in their functional states. Although this plasticity is essential to their function, little is known about the dynamics underlying...
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NMR-Based Molecular view of the Biology and Biophysics of WIP, An Intrinsically Disordered Protein
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Publication date: 16 February 2016
Source:Biophysical Journal, Volume 110, Issue 3, Supplement 1</br>
Author(s): Eva Rozentur-Shkop, Hadassa Shaked, Jordan Chill</br>
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[NMR paper] Visualizing the molecular recognition trajectory of an intrinsically disordered protein using multinuclear relaxation dispersion NMR.
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http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Visualizing the molecular recognition trajectory of an intrinsically disordered protein using multinuclear relaxation dispersion NMR.
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Authors: Schneider R, Maurin D, Communie G, Kragelj J, Hansen DF, Ruigrok RW, Jensen MR, Blackledge M
Abstract
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4D Non-uniformly sampled HCBCACON and 1J(NCα)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins
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Abstract A pair of 4D NMR experiments for the backbone assignment of disordered proteins is presented. The experiments exploit 13C direct detection and non-uniform sampling of the indirectly detected dimensions, and provide correlations of the aliphatic proton (Hα, and Hβ) and carbon (Cα, Cβ) resonance frequencies to the protein backbone. Thus, all the chemical shifts regularly used to map the transient...
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[NMR paper] NMR solution structure of the pathogenesis-related protein P14a.
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J Mol Biol. 1997 Feb 28;266(3):576-93
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The nuclear magnetic resonance (NMR) structure of the 15 kDa pathogenesis-related protein P14a, which displays antifungicidal activity and is induced in tomato leaves as a...
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[NMR paper] NMR solution structure of the pathogenesis-related protein P14a.
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J Mol Biol. 1997 Feb 28;266(3):576-93
Authors: Fernández C, Szyperski T, Bruyère T, Ramage P, Mösinger E, Wüthrich K
The nuclear magnetic resonance (NMR) structure of the 15 kDa pathogenesis-related protein P14a, which displays antifungicidal activity and is induced in tomato leaves as a...
Common molecular pathogenesis of disease-related intrinsically disordered proteins revealed by NMR analysis.
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