Related ArticlesDistinct 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
The residual solution structures of two alpha-synuclein mutants, A30P and A53T, observed in family members of patients with Parkinson's disease were compared with that of wild-type by NMR. The A53T substitution had been shown to accelerate fibril formation of alpha-synuclein, whereas the A30P mutation has the negative and positive effects on the formation of the fibril and spherical oligomer, respectively. The remaining structure was analyzed via amide-proton exchange and signal intensity measurements using NMR. Amide-proton exchange was used for both the calculation of kex values and ratio of kex at different temperatures. Effects of the A30P (N-terminal region) mutation were observed at the C-terminal region as a more flexible structure, suggesting that long-range interactions exist between the N- and C-terminal regions in alpha-synuclein. In addition, the N-terminal region adopted a more rigid structure in the A53T and A30P mutants than in the wild-type. It was concluded that the structural change caused by the mutations is related to the formation of a beta-hairpin at the initiation site of the N-terminal core structure. Furthermore, the signal intensity was used to estimate the rigidity of the structure. Higher signal intensities were observed for A30P at the 112, 113, and 116C-terminal residues, suggesting that this region adopts more flexible structure. The ratio of the intensities at different temperatures indicated more flexible or rigid structures in the N-terminal region of A30P than in that of wild-type. Thus, using different approaches and temperatures is a good method to analyze residual structure in intrinsically disordered proteins.
PMID: 32497661 [PubMed - as supplied by publisher]
[NMR paper] Comparison of residual alpha- and beta-structures between two intrinsically disordered proteins by using NMR.
Comparison of residual alpha- and beta-structures between two intrinsically disordered proteins by using NMR.
Comparison of residual alpha- and beta-structures between two intrinsically disordered proteins by using NMR.
Biochim Biophys Acta. 2014 Dec 15;
Authors: Ono Y, Miyashita M, Ono Y, Okazaki H, Watanabe S, Tochio N, Kigawa T, Nishimura C
Abstract
Intrinsically disordered proteins contain some residual structures, which may fold further upon binding to the partner protein for function. The residual structures observed in...
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Comparison of residual alpha- and beta-structures between two intrinsically disordered proteins by using NMR
Comparison of residual alpha- and beta-structures between two intrinsically disordered proteins by using NMR
Publication date: Available online 15 December 2014
Source:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics</br>
Author(s): Yu-ichi Ono , Manami Miyashita , Yumi Ono , Honoka Okazaki , Satoru Watanabe , Naoya Tochio , Takanori Kigawa , Chiaki Nishimura</br>
Intrinsically disordered proteins contain some residual structures, which may fold further upon binding to the partner protein for function. The residual structures observed in two...
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12-16-2014 03:47 AM
[NMR paper] 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.
Related Articles Flexible and Rigid Structures in HIV-1 p17 Matrix Protein Monitored by Relaxation and Amide Proton Exchange with NMR.
Biochim Biophys Acta. 2013 Dec 26;
Authors: Ohori Y, Okazaki H, Watanabe S, Tochio N, Arai M, Kigawa T, Nishimura C
Abstract
The HIV-1 p17 matrix protein is a multifunctional protein that interacts with other molecules including proteins and membranes. The dynamic structure between its...
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01-01-2014 03:05 PM
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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12-26-2013 10:21 PM
[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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10-12-2013 05:24 PM
[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: ...
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[NMR paper] Kinetics of amide proton exchange in parvalbumin studied by 1H 2-D NMR. A comparison
Kinetics of amide proton exchange in parvalbumin studied by 1H 2-D NMR. A comparison of the calcium and magnesium loaded forms.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Kinetics of amide proton exchange in parvalbumin studied by 1H 2-D NMR. A comparison of the calcium and magnesium loaded forms.
Biochimie. 1992 Sep-Oct;74(9-10):837-44
Authors: Baldellon C, Padilla A, Cavé A
The amide proton exchange rates have been measured for the pike parvalbumin loaded...
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[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...
Distinct residual and disordered structures of alpha-synuclein analyzed by amide-proton exchange and NMR signal intensity.
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