Solid-state and unilateral NMR study of deterioration of a Dead Sea Scroll fragment.
Anal Bioanal Chem. 2011 Jul 30;
Authors: Masic A, Chierotti MR, Gobetto R, Martra G, Rabin I, Coluccia S
Unilateral and solid-state nuclear magnetic resonance (NMR) analyses were performed on a parchment fragment of the Dead Sea Scroll (DSS). The analyzed sample belongs to the collection of non-inscribed and nontreated fragments of known archaeological provenance from the John Rylands University Library in Manchester. Therefore, it can be considered as original DSS material free from any contamination related to the post-discovery period. Considering the paramount significance of the DSS, noninvasive approaches and portable in situ nondestructive methods are of fundamental importance for the determination of composition, structure, and chemical-physical properties of the materials under study. NMR studies reveal low amounts of water content associated with very short proton relaxation times, T (1), indicating a high level of deterioration of collagen molecules within scroll fragments. In addition, (13)C cross-polarization magic-angle-spinning (CPMAS) NMR spectroscopy shows characteristic peaks of lipids whose presence we attribute to the production technology that did not involve liming. Extraction with chloroform led to the reduction of both lipid and protein signals in the (13)C CPMAS spectrum indicating probable involvement of lipids in parchment degradation processes. NMR absorption and relaxation measurements provide nondestructive, discriminative, and sensitive tools for studying the deterioration effects on the organization and properties of water and collagen within ancient manuscripts.
PMID: 21805064 [PubMed - as supplied by publisher]
[NMR paper] 15N and 31P solid-state NMR study of transmembrane domain alignment of M2 protein of
15N and 31P solid-state NMR study of transmembrane domain alignment of M2 protein of influenza A virus in hydrated cylindrical lipid bilayers confined to anodic aluminum oxide nanopores.
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J Magn Reson. 2005 Apr;173(2):322-7
Authors: Chekmenev EY, Hu J, Gor'kov PL, Brey WW, Cross TA, Ruuge A, Smirnov AI
This communication reports the first...
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[NMR paper] Solid-state NMR studies of the secondary structure of a mutant prion protein fragment
Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration.
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Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11686-90
Authors: Laws DD, Bitter HM, Liu K, Ball HL, Kaneko K, Wille H, Cohen FE, Prusiner SB, Pines A, Wemmer DE
The secondary structure of a 55-residue fragment of the mouse prion protein, MoPrP(89-143), was studied in...
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11-19-2010 08:44 PM
[NMR paper] A solid-state NMR study of protein hydration and stability.
A solid-state NMR study of protein hydration and stability.
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Pharm Res. 1998 Dec;15(12):1816-21
Authors: Separovic F, Lam YH, Ke X, Chan HK
PURPOSE: The mobility of protein in powders at different hydration levels was studied in relation to aggregation and activity. METHODS: Magic angle spinning 13C, 15N, 1H, 2H, and 17O NMR techniques were used to determine changes in the mobility of surface residues in proteins as a function of hydration and related to changes in...
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[NMR paper] Dynamic structure of proteins in solid state. 1H and 13C NMR relaxation study.
Dynamic structure of proteins in solid state. 1H and 13C NMR relaxation study.
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J Biomol Struct Dyn. 1996 Oct;14(2):211-24
Authors: Krushelnitsky AG, Fedotov VD, Spevacek J, Straka J
Temperature dependencies of 1H non-selective NMR T1 and T2 relaxation times measured at two resonance frequencies and natural abundance 13C NMR relaxation times T1 and T1r measured at room temperature have been studied in a set of dry and wet solid proteins - Bacterial...
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[NMR paper] Solid-state NMR studies of the prion protein H1 fragment.
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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 Solid-state NMR studies of the prion protein H1 fragment.
Protein Sci. 1996 Aug;5(8):1655-61
Authors: Heller J, Kolbert AC, Larsen R, Ernst M, Bekker T, Baldwin M, Prusiner SB, Pines A, Wemmer DE
Conformational...
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[NMR paper] Solid-state 13C and 15N NMR study of the low pH forms of bacteriorhodopsin.
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Biochemistry. 1990 Jul 24;29(29):6873-83
Authors: de Groot HJ, Smith SO, Courtin J, van den Berg E, Winkel C, Lugtenburg J, Griffin RG, Herzfeld J
The visible absorption of bacteriorhodopsin (bR) is highly sensitive to pH, the maximum shifting from 568 nm (pH 7) to approximately 600 nm (pH 2) and back to 565 nm (pH 0) as the pH is decreased further with HCl. Blue membrane...
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[NMR paper] Solid-state 13C NMR study of tyrosine protonation in dark-adapted bacteriorhodopsin.
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Authors: Herzfeld J, Das Gupta SK, Farrar MR, Harbison GS, McDermott AE, Pelletier SL, Raleigh DP, Smith SO, Winkel C, Lugtenburg J
Solid-state 13C MAS NMR spectra were obtained for dark-adapted bacteriorhodopsin (bR) labeled with Tyr. Difference spectra (labeled minus natural abundance) taken at pH values between 2 and...
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A Solid-State (17)O NMR Study of l-Tyrosine in Different Ionization States: Implicati
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J Phys Chem B. 2010 Aug 16;
Authors: Zhu J, Lau JY, Wu G
We report experimental characterization of (17)O quadrupole coupling (QC) and chemical shift (CS) tensors for the phenolic oxygen in three l-tyrosine (l-Tyr) compounds: l-Tyr, l-Tyr.HCl, and Na(2)(l-Tyr)....