Related ArticlesThe 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 temperature and from an aqueous solution. The primary structure is mainly Ala-Gly alternative copolypeptide, but Gly-Ala-Ala-Ser units appear frequently and periodically. Thus, this study aims at elucidating the role of such Gly-Ala-Ala-Ser units on the secondary structure. The sequential model peptides containing Gly-Ala-Ala-Ser units selected from the primary structure of B. mori silk fibroin were synthesized, and their secondary structure was studied with (13)C CP/MAS NMR and wide-angle X-ray scattering. The (13)C isotope labeling of the peptides and the (13)C conformation-dependent chemical shifts were used for the purpose. The Ala-Ala units take antiparallel beta-sheet structure locally, and the introduction of one Ala-Ala unit in (Ala-Gly)(15) chain promotes dramatical structural changes from silk I (repeated beta-turn type II structure) to silk II (antiparallel beta-sheet structure). Thus, the presence of Ala-Ala units in B. mori silk fibroin chain will be one of the inducing factors of the structural transition for silk fiber formation. The role of Tyr residue in the peptide chain was also studied and clarified to induce "locally nonordered structure."
Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.
Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.
Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.
Eur Biophys J. 2011 Jan 28;
Authors: Grasnick D, Sternberg U, Strandberg E, Wadhwani P, Ulrich AS
To better understand peptide-induced membrane fusion at a molecular level, we set out to determine the structure of the fusogenic peptide FP23 from the HIV-1 protein gp41 when bound to a lipid bilayer. An established solid-state...
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[NMR paper] Structural analysis of Bombyx mori silk fibroin peptides with formic acid treatment u
Structural analysis of Bombyx mori silk fibroin peptides with formic acid treatment using high-resolution solid-state 13C NMR spectroscopy.
Related Articles Structural 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...
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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] 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] Solid-state NMR determination of the secondary structure of Samia cynthia ricini silk
Solid-state NMR determination of the secondary structure of Samia cynthia ricini silk.
Related Articles Solid-state NMR determination of the secondary structure of Samia cynthia ricini silk.
Nature. 2000 Jun 29;405(6790):1077-9
Authors: van Beek JD, Beaulieu L, Schäfer H, Demura M, Asakura T, Meier BH
Silks are fibrous proteins that form heterogeneous, semi-crystalline solids. Silk proteins have a variety of physical properties reflecting their range of functions. Spider dragline silk, for example, has high tensile strength and elasticity,...
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11-18-2010 09:15 PM
[NMR paper] 1H, 15N, 13C and 13CO assignments and secondary structure determination of basic fibr
1H, 15N, 13C and 13CO assignments and secondary structure determination of basic fibroblast growth factor using 3D heteronuclear NMR spectroscopy.
Related Articles 1H, 15N, 13C and 13CO assignments and secondary structure determination of basic fibroblast growth factor using 3D heteronuclear NMR spectroscopy.
J Biomol NMR. 1995 Nov;6(3):245-54
Authors: Moy FJ, Seddon AP, Campbell EB, Böhlen P, Powers R
The assignments of the 1H, 15N, 13CO and 13C resonances of recombinant human basic fibroblast growth factor (FGF-2), a protein comprising of...
The role of irregular unit, GAAS, on the secondary structure of Bombyx mori silk fibr
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