Abstract
Wings of flying insects are part of the cuticle which forms the exoskeleton. The primary molecular components of cuticle are protein, chitin, and lipid. How these components interact with one another to form the exoskeleton is not completely understood. The difficulty in characterizing the cuticle arises because it is insoluble and noncrystalline. These properties severely limit the experimental tools that can be used for molecular characterization. Solid-state nuclear magnetic resonance experiments have been used in the past to characterize the exoskeleton of beetles and have found that chitin and protein make comparable contributions to the molecular matrix. However, little work has been done to characterize the components of the wing, which includes vein and membrane. In this work, solid-state NMR was used to characterize the wing of the 17-year cycle cicada (Magicicada cassini) that appeared in northern West Virginia during the summer of 2016. The NMR results show noticeable differences between the molecular components of the vein and membrane.
PMID: 28727439 [PubMed - as supplied by publisher]
[NMR paper] Solid state deuterium NMR study of LK?14 peptide aggregation in biosilica.
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Biointerphases. 2017 Jun 27;12(2):02D418
Authors: Ferreira HE, Drobny GP
Abstract
In nature, organisms including diatoms, radiolaria, and marine sponges use proteins, long chain polyamines, and other organic molecules to regulate the assembly of complex silica-based structures. Here, the authors investigate structural features of small peptides, designed to mimic...
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[NMR paper] How high concentrations of proteins stabilize the amorphous state of calcium orthophosphate: a solid-state NMR study of the casein case.
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Langmuir. 2017 Jan 17;:
Authors: De Sa Peixoto P, Silva JV, Laurent GP, Schmutz M, Thomas D, Bouchoux A, Gesan-Guiziou G
Abstract
Understanding how proteins stabilize Amorphous Calcium ortho-Phosphate (ACP) phases is of great importance in...
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[NMR paper] Solid-state NMR Spectroscopy to Study Protein-Lipid Interactions.
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Biochim Biophys Acta. 2013 Dec 11;
Authors: Huster D
Abstract
The appropriate lipid environment is crucial for the proper function of membrane proteins. There is a tremendous variety of lipid molecules in the membrane and so far it is often unclear which component of the lipid matrix is essential for the function of a respective protein. Lipid molecules and proteins mutually influence...
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Solid-state NMR Spectroscopy to Study Protein-Lipid Interactions
Solid-state NMR Spectroscopy to Study Protein-Lipid Interactions
Publication date: Available online 12 December 2013
Source:Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids</br>
Author(s): Daniel Huster</br>
The appropriate lipid environment is crucial for the proper function of membrane proteins. There is a tremendous variety of lipid molecules in the membrane and so far it is often unclear which component of the lipid matrix is essential for the function of a respective protein. Lipid molecules and proteins mutually influence each other;...
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[NMR paper] 15N and 31P solid-state NMR study of transmembrane domain alignment of M2 protein of
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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] 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.
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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 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...