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J Neurochem. 1994 Jan;62(1):349-54
Authors: Klunk WE, Xu CJ, Pettegrew JW
The beta/A4-amyloid protein (beta/A4) and many synthetic fragments of this protein have proved to be very difficult to solubilize, leading to the use of relatively harsh chemical methods, most notably, formic acid. This treatment has previously been shown to cause a covalent modification of this peptide. In this study, one- and two-dimensional NMR techniques are used to show that the nature of this covalent modification is formation of a formate ester to a serine residue. This finding is consistent with our previously reported kinetic studies of formic acid-induced modification of beta/A4 and further illustrates the potential danger of solubilizing fragments of beta/A4 in formic acid. Alternative methods of solubilization are discussed.
Solid-state NMR analysis of interaction sites of curcumin and 42-residue amyloid ?-protein fibrils.
Solid-state NMR analysis of interaction sites of curcumin and 42-residue amyloid ?-protein fibrils.
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Bioorg Med Chem. 2011 Aug 27;
Authors: Masuda Y, Fukuchi M, Yatagawa T, Tada M, Takeda K, Irie K, Akagi KI, Monobe Y, Imazawa T, Takegoshi K
Abstract
Aggregation of 42-residue amyloid ?-protein (A?42) plays a pivotal role in the etiology of Alzheimer's disease (AD). Curcumin, the yellow pigment in the rhizome of turmeric, attracts...
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Expression and purification of (15)N- and (13)C-isotope labeled 40-residue human Alzheimer's ?-amyloid peptide for NMR-based structural analysis.
Expression and purification of (15)N- and (13)C-isotope labeled 40-residue human Alzheimer's ?-amyloid peptide for NMR-based structural analysis.
Expression and purification of (15)N- and (13)C-isotope labeled 40-residue human Alzheimer's ?-amyloid peptide for NMR-based structural analysis.
Protein Expr Purif. 2011 May 27;
Authors: Long F, Cho W, Ishii Y
Amyloid fibrils of Alzheimer's ?-amyloid peptide (A?) are a primary component of amyloid plaques, a hallmark of Alzheimer's disease (AD). Enormous attention has been given to the structural...
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[Question from NMRWiki Q&A forum] Aminoacid residue identification or assignment of protein from 3D NMR Experments
Aminoacid residue identification or assignment of protein from 3D NMR Experments
Dear NMR Wiki'ers
I am identifying aminoacid residues or assignment of protein from following 3D NMR experments
HNCA/HNCOCA - Glycine (45 ppm )
CBCANH/CBCACONH - Alanine (52-CA , 19 - CB ), Serine,threonine - ( CA-58.57 , CB - 64 or 70 )
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[NMR paper] NMR identification of the formic acid-modified residue in Alzheimer's amyloid protein
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles NMR identification of the formic acid-modified residue in Alzheimer's amyloid protein.
J Neurochem. 1994 Jan;62(1):349-54
Authors: Klunk WE, Xu CJ, Pettegrew JW
The beta/A4-amyloid protein (beta/A4) and many synthetic fragments of this protein have proved to be very difficult to solubilize, leading to...
nmrlearner
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[NMR paper] An unusual peptide conformation may precipitate amyloid formation in Alzheimer's dise
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Biochemistry. 1991 Oct 29;30(43):10382-7
Authors: Spencer RG, Halverson KJ, Auger M, McDermott AE, Griffin RG, Lansbury PT
The formation of insoluble proteinaceous deposits is...
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[NMR paper] An unusual peptide conformation may precipitate amyloid formation in Alzheimer's dise
An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: application of solid-state NMR to the determination of protein secondary structure.
Related Articles An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: application of solid-state NMR to the determination of protein secondary structure.
Biochemistry. 1991 Oct 29;30(43):10382-7
Authors: Spencer RG, Halverson KJ, Auger M, McDermott AE, Griffin RG, Lansbury PT
The formation of insoluble proteinaceous deposits is...
NMR identification of the formic acid-modified residue in Alzheimer's amyloid protein
Linear Mode
