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Cited by 487

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Isolation of a clone encoding a second dragline silk fibroin. Nephila clavipes dragline silk is a two-protein fiber.

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Hinman, M.B., Lewis, R.V.·1992·Journal of Biological Chemistry

Abstract

Spider dragline silk is a unique protein fiber possessing both high tensile strength and high elasticity. A partial cDNA clone for one dragline silk protein (Spidroin 1) was previously isolated. However, the predicted amino acid sequence could not account for the amino acid composition of dragline silk. We have isolated a partial cDNA clone for another dragline silk protein (Spidroin 2), demonstrating that dragline silk is composed of multiple proteins. The amino acid sequence exhibits an entirely different repetitive motif than Spidroin 1. Spidroin 2 is predicted to consist of linked beta-turns in proline-rich regions which alternate with beta-sheet regions composed of polyalanine segments. This structure for Spidroin 2 provides a model for dragline silk structure and function.

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Metadata

Authors
Hinman, M. B., & Lewis, R. V.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1992-09
Volume
267
Issue
27
Pages
19320-19324
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1542008397
Cited by
487
References
0
FWCI
3.52
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Isolation of a clone encoding a second dragline silk fibroin. Nephila clavipes dragline silk is a two-protein fiber. https://app.cochat.ai/papers/10.1016/s0021-9258(18)41777-2
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Hinman, M. B., & Lewis, R. V. (1992). Isolation of a clone encoding a second dragline silk fibroin. Nephila clavipes dragline silk is a two-protein fiber. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)41777-2

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.