Related Articles13C NMR of Nephila clavipes major ampullate silk gland.
Biophys J. 1996 Dec;71(6):3442-7
Authors: Hijirida DH, Do KG, Michal C, Wong S, Zax D, Jelinski LW
The major ampullate glands of the spider Nephila clavipes contain approximately 0.2 microliter each of a highly concentrated (approximately 50%) solution of silk fibroin. Therefore, the reservoir of silk in these glands presents an ideal opportunity to observe prefolded conformations of a protein in its native state. To this end, the structure and conformation of major ampullate gland silk fibroin within the glands of the spider N. clavipes were examined by 13C NMR spectroscopy. These results were compared to those from silk protein first drawn from the spinneret and then denatured. The 13C NMR chemical shifts, along with infrared and circular dichroism data, suggest that the silk fibroin in the glands exists in dynamically averaged helical conformations. Furthermore, there is no evidence of proline residues in U-(13)C-D-glucose-labeled silk. This transient prefolded "molten fibril" state may correspond to the silk I form found in Bombyx mori silk. There is no evidence of the final beta-sheet structure in the ampullate gland silk fibroin before final silk processing. However, the conformation of silk in the glands appears to be in a highly metastable state, as plasticization with water produces the beta-sheet structure. Therefore, the ducts connecting the ampullate glands to the spinnerets play a larger role in silk processing than previously thought.
NMR assignments of the N-terminal domain of Nephila clavipes spidroin 1.
NMR assignments of the N-terminal domain of Nephila clavipes spidroin 1.
NMR assignments of the N-terminal domain of Nephila clavipes spidroin 1.
Biomol NMR Assign. 2010 Dec 10;
Authors: Parnham S, Gaines WA, Duggan BM, Marcotte WR, Hennig M
The building blocks of spider dragline silk are two fibrous proteins secreted from the major ampullate gland named spidroins 1 and 2 (MaSp1, MaSp2). These proteins consist of a large central domain composed of approximately 100 tandem copies of a 35-40 amino acid repeat sequence. Non-repetitive N and...
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[NMR paper] Design, expression and solid-state NMR characterization of silk-like materials constr
Design, expression and solid-state NMR characterization of silk-like materials constructed from sequences of spider silk, Samia cynthia ricini and Bombyx mori silk fibroins.
Related Articles Design, expression and solid-state NMR characterization of silk-like materials constructed from sequences of spider silk, Samia cynthia ricini and Bombyx mori silk fibroins.
J Biochem. 2005 Jun;137(6):721-9
Authors: Yang M, Asakura T
Silk has a long history of use in medicine as sutures. To address the requirements of a mechanically robust and...
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11-25-2010 08:21 PM
[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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[NMR paper] NMR characterization of native liquid spider dragline silk from Nephila edulis.
NMR characterization of native liquid spider dragline silk from Nephila edulis.
Related Articles NMR characterization of native liquid spider dragline silk from Nephila edulis.
Biomacromolecules. 2004 May-Jun;5(3):834-9
Authors: Hronska M, van Beek JD, Williamson PT, Vollrath F, Meier BH
Solid spider dragline silk is well-known for its mechanical properties. Nonetheless a detailed picture of the spinning process is lacking. Here we report NMR studies on the liquid silk within the wide sac of the major ampullate (m.a.) gland from the spider...
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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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[NMR paper] Supercontracted spider dragline silk: a solid-state NMR study of the local structure.
Supercontracted spider dragline silk: a solid-state NMR study of the local structure.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Supercontracted spider dragline silk: a solid-state NMR study of the local structure.
Int J Biol Macromol. 1999 Mar-Apr;24(2-3):173-8
Authors: van Beek JD, Kümmerlen J, Vollrath F, Meier BH
The local structure of supercontracted dragline silk from the spider Nephila madagascariensis was investigated by solid-state nuclear magnetic...
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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...