Related ArticlesStructural analysis of Bombyx mori silk fibroin peptides with formic acid treatment using high-resolution solid-state 13C NMR spectroscopy.
Biomacromolecules. 2004 Sep-Oct;5(5):1763-9
Authors: Yao J, Ohgo K, Sugino R, Kishore R, Asakura T
Bombyx mori silk fibroin fiber is a fibrous protein produced by the silkworm at room temperature and from an aqueous solution whose primary structure is highly repetitive. In this study we analyzed the structural characteristics of native peptides, derived from B. mori silk fibroin, with formic acid treatment using high-resolution solid-state 13C NMR. We establish that the Ser residue bearing a short polar side chain has the ability to stabilize the conformation formed in the model peptides due to its ability to form intermolecular hydrogen bonds involving its hydroxyl group as a donor and the carbonyl groups of other residues as acceptors. On the other hand, insertion of Tyr residue in the basic (AG)n and (AGSGAG)n sequence motifs usually exhibited disruptive effects on the preferred conformations. Moreover, the environmental effect was investigated by mixing the native Cp fraction with the model peptides, showing that there is no significant structural difference on the Ser-containing peptides, while structural transformation was observed on the peptides containing the GAAS unit. This may be attributed to the fact that the Cp fraction promotes the formation of an antiparallel beta-sheet in the Ala-Ala unit. Such periodically disrupted ordered structures in the semicrystalline region of B. mori silk fibroin may be critical not only for facilitating the conformational transformation from silk I to silk II structural form but also for having some correlation with the unique properties of the silk materials.
[NMR paper] Effect of pH and copper(II) on the conformation transitions of silk fibroin based on
Effect of pH and copper(II) on the conformation transitions of silk fibroin based on EPR, NMR, and Raman spectroscopy.
Related Articles Effect of pH and copper(II) on the conformation transitions of silk fibroin based on EPR, NMR, and Raman spectroscopy.
Biochemistry. 2004 Sep 28;43(38):11932-41
Authors: Zong XH, Zhou P, Shao ZZ, Chen SM, Chen X, Hu BW, Deng F, Yao WH
Much attention has been paid to the natural mechanism of silkworm spinning due to the impressive mechanical properties of the natural fibers. Our results in the present work show...
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11-24-2010 10:01 PM
[NMR paper] Structure of the model peptides of Bombyx mori silk-elastin like protein studied with
Structure of the model peptides of Bombyx mori silk-elastin like protein studied with solid state NMR.
Related Articles Structure of the model peptides of Bombyx mori silk-elastin like protein studied with solid state NMR.
Biomacromolecules. 2004 May-Jun;5(3):744-50
Authors: Ohgo K, Kurano TL, Kumashiro KK, Asakura T
The peptides (AG)(6)(VPGVG)(AG)(7) and (AG)(5)(VPGVG)(2)(AG)(5) are models for a new type of protein with both composition and properties such as Bombyx mori silk and elastin. In this paper, we report the solid-state NMR results...
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11-24-2010 09:51 PM
[NMR paper] Structural role of tyrosine in Bombyx mori silk fibroin, studied by solid-state NMR a
Structural role of tyrosine in Bombyx mori silk fibroin, studied by solid-state NMR and molecular mechanics on a model peptide prepared as silk I and II.
Related Articles Structural role of tyrosine in Bombyx mori silk fibroin, studied by solid-state NMR and molecular mechanics on a model peptide prepared as silk I and II.
Magn Reson Chem. 2004 Feb;42(2):258-66
Authors: Asakura T, Suita K, Kameda T, Afonin S, Ulrich AS
The influence of the bulky and H-bonding Tyr side-chain on its Ala- and Gly-rich environment in Bombyx mori silk fibroin was...
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11-24-2010 09:25 PM
[NMR paper] NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiologica
NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH.
Related Articles NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH.
FEBS Lett. 2002 Nov 6;531(2):314-8
Authors: Lee D, Damberger FF, Peng G, Horst R, Güntert P, Nikonova L, Leal WS, Wüthrich K
The nuclear magnetic resonance structure of the unliganded pheromone-binding protein (PBP) from Bombyx mori at pH above 6.5, BmPBP(B), consists of seven helices with residues 3-8, 16-22, 29-32, 46-59, 70-79, 84-100, and...
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[NMR paper] The role of irregular unit, GAAS, on the secondary structure of Bombyx mori silk fibr
The role of irregular unit, GAAS, on the secondary structure of Bombyx mori silk fibroin studied with 13C CP/MAS NMR and wide-angle X-ray scattering.
Related Articles The role of irregular unit, GAAS, on the secondary structure of Bombyx mori silk fibroin studied with 13C CP/MAS NMR and wide-angle X-ray scattering.
Protein Sci. 2002 Aug;11(8):1873-7
Authors: Asakura T, Sugino R, Okumura T, Nakazawa Y
Bombyx mori silk fibroin is a fibrous protein whose fiber is extremely strong and tough, although it is produced by the silkworm at room...
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[NMR paper] NMR assignment of the A form of the pheromone-binding protein of Bombyx mori.
NMR assignment of the A form of the pheromone-binding protein of Bombyx mori.
Related Articles NMR assignment of the A form of the pheromone-binding protein of Bombyx mori.
J Biomol NMR. 2001 Jan;19(1):79-80
Authors: Horst R, Damberger F, Peng G, Nikonova L, Leal WS, Wüthrich K
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11-19-2010 08:32 PM
[NMR paper] NMR identification of the formic acid-modified residue in Alzheimer's amyloid protein
NMR identification of the formic acid-modified residue in Alzheimer's amyloid protein.
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...
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[NMR paper] Structural analysis of silk with 13C NMR chemical shift contour plots.
Structural analysis of silk with 13C NMR chemical shift contour plots.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structural analysis of silk with 13C NMR chemical shift contour plots.
Int J Biol Macromol. 1999 Mar-Apr;24(2-3):167-71
Authors: Asakura T, Iwadate M, Demura M, Williamson MP
The polymorphic structures of silk fibroins in the solid state were examined on the basis of a quantitative relationship between the 13C chemical shift and local structure in...
Structural analysis of Bombyx mori silk fibroin peptides with formic acid treatment u
Linear Mode
