Investigation of the nanofibrils of silk fibers

Putthanarat, S.; Stribeck, Norbert; Fossey, Stephen A.; Eby, R. K.; Adams, W. Wade

doi:10.1016/s0032-3861(00)00036-7

Cited by 142 publications

(121 citation statements)

References 37 publications

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“…Note that previous results have indicated that the local structure is not significantly altered on supercontraction (48). Recently, evidence for the existence of fibrillar substructures in silk thread has been presented (20,21). Such substructures are consistent with our data, as long as the fibrils are parallel and oriented along the fiber (20), which was indeed observed.…”

Section: Biophysicssupporting

confidence: 93%

“…Recently, evidence for the existence of fibrillar substructures in silk thread has been presented (20,21). Such substructures are consistent with our data, as long as the fibrils are parallel and oriented along the fiber (20), which was indeed observed. Much broader distributions in the DECODER experiment would be observed when not fulfilling this constraint.…”

Section: Biophysicssupporting

confidence: 92%

“…Such polymorphic behavior is often found in proteins (19). Structures in silk, beyond the secondary structure, include tertiary structure and the possible formation of supramolecular helices, microcrystals and a microfibrillar organization of the silk fiber (11,20,21).…”

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confidence: 99%

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The molecular structure of spider dragline silk: Folding and orientation of the protein backbone

Beek

Heß

Vollrath

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

481

607

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The design principles of spider dragline silk, nature's highperformance fiber, are still largely unknown, in particular for the noncrystalline glycine-rich domains, which form the bulk of the material. Here we apply two-dimensional solid-state NMR to determine the distribution of the backbone torsion angles ( , ) as well as the orientation of the polypeptide backbone toward the fiber at both the glycine and alanine residues. Instead of an ''amorphous matrix,'' suggested earlier for the glycine-rich domains, these new data indicate that all domains in dragline silk have a preferred secondary structure and are strongly oriented, with the chains predominantly parallel to the fiber. As proposed previously, the alanine residues are predominantly found in a ␤ sheet conformation. The glycine residues are partly incorporated into the ␤ sheets and otherwise form helical structures with an approximate 3-fold symmetry.

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Section: Biophysicssupporting

confidence: 93%

Section: Biophysicssupporting

confidence: 92%

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The molecular structure of spider dragline silk: Folding and orientation of the protein backbone

Beek

Heß

Vollrath

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

481

607

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“…As a result, only a few techniques can provide structural information about silk monofilaments, including microscopic methods (atomic force microscopy, [1][2][3][4][5][6] scanning 3,5 and transmission electron microscopy, 7,8 and scanning transmission X-ray microscopy 9,10 ) and synchrotron X-ray diffraction. 11,12 Nevertheless, some of these techniques require a certain degree of treatment of the fiber that might affect its structure and/or they provide no molecular (i.e., spectroscopic) information.…”

Section: Introductionmentioning

confidence: 99%

Structure of silk by raman spectromicroscopy: From the spinning glands to the fibers

et al. 2011

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Raman spectroscopy has long been proved to be a useful tool to study the conformation of protein‐based materials such as silk. Thanks to recent developments, linearly polarized Raman spectromicroscopy has appeared very efficient to characterize the molecular structure of native single silk fibers and spinning dopes because it can provide information relative to the protein secondary structure, molecular orientation, and amino acid composition. This review will describe recent advances in the study of the structure of silk by Raman spectromicroscopy. A particular emphasis is put on the spider dragline and silkworm cocoon threads, other fibers spun by orb‐weaving spiders, the spinning dope contained in their silk glands and the effect of mechanical deformation. Taken together, the results of the literature show that Raman spectromicroscopy is particularly efficient to investigate all aspects of silk structure and production. The data provided can lead to a better understanding of the structure of the silk dope, transformations occurring during the spinning process, and structure and mechanical properties of native fibers. © 2011 Wiley Periodicals, Inc. Biopolymers 97: 322–336, 2012.

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“…This situation can be overcome by inclining the reinforcing microfibrils with respect to the principal axis of the material. This principle is observed in the nature where reinforcing fibrils are frequently inclined with respect to the principal axis of fibers found both in fauna [63] and flora [64,65]. Man-made model systems that both show similar scattering patterns, and in which the microfibrillar angle can easily be adjusted have been prepared and a feasibility study [66] has been performed utilizing USAXS at HASYLAB, beamline BW4 in different states of elongation.…”

Section: Orientation Of Nanofibrils In Highly Oriented Polymer Blendsmentioning

confidence: 99%

Investigation of the nanofibrils of silk fibers

Cited by 142 publications

References 37 publications

The molecular structure of spider dragline silk: Folding and orientation of the protein backbone

The molecular structure of spider dragline silk: Folding and orientation of the protein backbone

Structure of silk by raman spectromicroscopy: From the spinning glands to the fibers

Deformation Behavior of Nanocomposites Studied by X-Ray Scattering: Instrumentation and Methodology

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