Related ArticlesGlycerin-Induced Conformational Changes in Bombyx mori Silk Fibroin Film Monitored by (13)C CP/MAS NMR and ¹H DQMAS NMR.
Int J Mol Sci. 2016 Sep 09;17(9):
Authors: Asakura T, Endo M, Hirayama M, Arai H, Aoki A, Tasei Y
Abstract
In order to improve the stiff and brittle characteristics of pure Bombyx mori (B. mori) silk fibroin (SF) film in the dry state, glycerin (Glyc) has been used as a plasticizer. However, there have been very limited studies on the structural characterization of the Glyc-blended SF film. In this study, (13)C Cross Polarization/Magic Angle Spinning nuclear magnetic resonance (CP/MAS NMR) was used to monitor the conformational changes in the films by changing the Glyc concentration. The presence of only 5 wt % Glyc in the film induced a significant conformational change in SF where Silk I* (repeated type II ?-turn and no ?-helix) newly appeared. Upon further increase in Glyc concentration, the percentage of Silk I* increased linearly up to 9 wt % Glyc and then tended to be almost constant (30%). This value (30%) was the same as the fraction of Ala residue within the Silk I* form out of all Ala residues of SF present in B. mori mature silkworm. The ¹H DQMAS NMR spectra of Glyc-blended SF films confirmed the appearance of Silk I* in the Glyc-blended SF film. A structural model of Glyc-SF complex including the Silk I* form was proposed with the guidance of the Molecular Dynamics (MD) simulation using ¹H-¹H distance constraints obtained from the ¹H Double-Quantum Magic Angle Spinning (DQMAS) NMR spectra.
[NMR paper] NMR Study of the Structures of Repeated Sequences, GAGXGA (X = S, Y, V), in Bombyx mori Liquid Silk.
NMR Study of the Structures of Repeated Sequences, GAGXGA (X = S, Y, V), in Bombyx mori Liquid Silk.
Related Articles NMR Study of the Structures of Repeated Sequences, GAGXGA (X = S, Y, V), in Bombyx mori Liquid Silk.
Biomacromolecules. 2013 Nov 22;
Authors: Suzuki Y, Yamazaki T, Aoki A, Shindo H, Asakura T
Abstract
The silk fibroin stored in the silk gland of Bombyx mori silkworm, called "liquid silk", is spun out and converted into the silk fiber with extremely high strength and high toughness. Therefore it is important to determine the...
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[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] 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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[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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[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