?-Synuclein (?S) is a presynaptic protein that binds to cell membranes and is linked to Parkinson's disease (PD). Binding of ?S to membranes is a likely first step in the molecular pathophysiology of PD. The ?S molecule can adopt multiple conformations, being largely disordered in water, adopting a ?-sheet conformation when present in amyloid fibrils, and forming a dynamic multiplicity of ?-helical conformations when bound to lipid bilayers and related membrane-mimetic surfaces. Multiscale...
[NMR paper] Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy.
Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy.
Related Articles Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy.
Biomolecules. 2020 Mar 10;10(3):
Authors: Kim DH, Lee J, Mok KH, Lee JH, Han KH
Abstract
Elucidating the structural details of proteins is highly valuable and important for the proper understanding of protein function. In the case of intrinsically disordered proteins (IDPs), however, obtaining the structural details is quite challenging, as the traditional...
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[NMR paper] Ca(2+) modulating ?-synuclein membrane transient interactions revealed by solution NMR spectroscopy.
Ca(2+) modulating ?-synuclein membrane transient interactions revealed by solution NMR spectroscopy.
Related Articles Ca(2+) modulating ?-synuclein membrane transient interactions revealed by solution NMR spectroscopy.
Biochim Biophys Acta. 2013 Dec 4;
Authors: Zhang Z, Dai C, Bai J, Xu G, Liu M, Li C
Abstract
?-synuclein is involved in Parkinson's disease and its interaction with cell membrane is crucial to its pathological and physiological functions. Membrane properties, such as curvature, lipid composition have been shown to affect the...
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[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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[NMR paper] Structure and orientation of bovine lactoferrampin in the mimetic bacterial membrane as revealed by solid-state NMR and molecular dynamics simulation.
Structure and orientation of bovine lactoferrampin in the mimetic bacterial membrane as revealed by solid-state NMR and molecular dynamics simulation.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles Structure and orientation of bovine lactoferrampin in the mimetic bacterial membrane as revealed by solid-state NMR and molecular dynamics simulation.
Biophys J. 2012 Oct 17;103(8):1735-43
Authors: Tsutsumi A, Javkhlantugs N, Kira A, Umeyama M, Kawamura I, Nishimura K, Ueda K,...
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[NMR paper] Temperature-dependent structural changes of Parkinson's alpha-synuclein reveal the role of pre-existing oligomers in alpha-synuclein fibrillization.
Temperature-dependent structural changes of Parkinson's alpha-synuclein reveal the role of pre-existing oligomers in alpha-synuclein fibrillization.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Temperature-dependent structural changes of Parkinson's alpha-synuclein reveal the role of pre-existing oligomers in alpha-synuclein fibrillization.
PLoS One. 2013;8(1):e53487
Authors: ...
Combining NMR ensembles and molecular dynamics simulations provides more realistic models of protein structures in solution and leads to better chemical shift prediction
Combining NMR ensembles and molecular dynamics simulations provides more realistic models of protein structures in solution and leads to better chemical shift prediction
Abstract While chemical shifts are invaluable for obtaining structural information from proteins, they also offer one of the rare ways to obtain information about protein dynamics. A necessary tool in transforming chemical shifts into structural and dynamic information is chemical shift prediction. In our previous work we developed a method for 4D prediction of protein 1H chemical shifts in which molecular motions, the...
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Membrane binding of an acyl-lactoferricin B antimicrobial peptide from solid-state NMR experiments and molecular dynamics simulations.
Membrane binding of an acyl-lactoferricin B antimicrobial peptide from solid-state NMR experiments and molecular dynamics simulations.
Membrane binding of an acyl-lactoferricin B antimicrobial peptide from solid-state NMR experiments and molecular dynamics simulations.
Biochim Biophys Acta. 2011 Aug;1808(8):2019-30
Authors: Romo TD, Bradney LA, Greathouse DV, Grossfield A
Abstract
One approach to the growing health problem of antibiotic resistant bacteria is the development of antimicrobial peptides (AMPs) as alternative treatments. The...
Membrane Interactions of alpha-Synuclein Revealed by Multiscale Molecular Dynamics Simulations, Markov State Models, and NMR
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