The aberrant aggregation of ?-synuclein (?S), a disordered protein primarily expressed in neuronal cells, is strongly associated with the underlying mechanisms of Parkinson's disease. It is now established that ?S has a weak affinity for metal ions and that these interactions alter its conformational properties by generally promoting self-assembly into amyloids. Here, we characterised the nature of the conformational changes associated with metal binding by ?S using nuclear magnetic resonance...
[NMR paper] Distinct residual and disordered structures of alpha-synuclein analyzed by amide-proton exchange and NMR signal intensity.
Distinct residual and disordered structures of alpha-synuclein analyzed by amide-proton exchange and NMR signal intensity.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Distinct residual and disordered structures of alpha-synuclein analyzed by amide-proton exchange and NMR signal intensity.
Biochim Biophys Acta Proteins Proteom. 2020 Jun 01;:140464
Authors: Okuwaki R, Shinmura I, Morita S, Matsugami A, Hayashi F, Goto Y, Nishimura C
Abstract
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Flexible and Rigid Structures in HIV-1 p17 Matrix Protein Monitored by Relaxation and Amide Proton Exchange with NMR
Flexible and Rigid Structures in HIV-1 p17 Matrix Protein Monitored by Relaxation and Amide Proton Exchange with NMR
Publication date: Available online 26 December 2013
Source:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics</br>
Author(s): Yuka Ohori , Honoka Okazaki , Satoru Watanabe , Naoya Tochio , Munehito Arai , Takanori Kigawa , Chiaki Nishimura</br>
The HIV-1 p17 matrix protein is a multifunctional protein that interacts with other molecules including proteins and membranes. The dynamic structure between its folded and partially unfolded...
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[NMR paper] Remaining structures at the N- and C-terminal regions of alpha-synuclein accurately elucidated by amide-proton exchange NMR with fitting.
Remaining structures at the N- and C-terminal regions of alpha-synuclein accurately elucidated by amide-proton exchange NMR with fitting.
Related Articles Remaining structures at the N- and C-terminal regions of alpha-synuclein accurately elucidated by amide-proton exchange NMR with fitting.
FEBS Lett. 2013 Oct 7;
Authors: Okazaki H, Ohori Y, Komoto M, Lee YH, Goto Y, Tochio N, Nishimura C
Abstract
Alpha-synuclein is analyzed in physiological conditions by CLEANEX-PM methodology, in which the amide-proton exchange can be monitored at...
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[NMR paper] Amide proton solvent protection in amylin fibrils probed by quenched hydrogen exchange NMR.
Amide proton solvent protection in amylin fibrils probed by quenched hydrogen exchange NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Amide proton solvent protection in amylin fibrils probed by quenched hydrogen exchange NMR.
PLoS One. 2013;8(2):e56467
Authors: Alexandrescu AT
Abstract
Amylin is an endocrine hormone that...
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[NMR paper] Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H N
Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra.
Related Articles Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra.
Protein Sci. 2000 Jan;9(1):186-93
Authors: Cavagnero S, Thériault Y, Narula SS, Dyson HJ, Wright PE
The hydrogen exchange behavior of exchangeable protons in proteins can provide important information for understanding the principles of protein structure and function. The positions and exchange rates of the slowly-exchanging amide...
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[NMR paper] Rapid amide proton exchange rates in peptides and proteins measured by solvent quench
Rapid amide proton exchange rates in peptides and proteins measured by solvent quenching and two-dimensional NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Rapid amide proton exchange rates in peptides and proteins measured by solvent quenching and two-dimensional NMR.
Protein Sci. 1995 Apr;4(4):804-14
Authors: Zhang YZ,...
[NMR paper] Comparison of amide proton exchange in reduced and oxidized Rhodobacter capsulatus cy
Comparison of amide proton exchange in reduced and oxidized Rhodobacter capsulatus cytochrome c2: a 1H-15N NMR study.
Related Articles Comparison of amide proton exchange in reduced and oxidized Rhodobacter capsulatus cytochrome c2: a 1H-15N NMR study.
J Biomol NMR. 1991 Jul;1(2):145-54
Authors: Gooley PR, Zhao D, MacKenzie NE
The hydrogen-deuterium exchange rates of the reduced and oxidized forms of Rhodobacter capsulatus cytochrome c2 were studied by 1H-15N homonuclear multiple quantum correlation spectroscopy. Minimal differences were...
Metal interactions of ?-synuclein probed by NMR amide-proton exchange
Linear Mode
