Evolutionary Divergence of Lepidopteran and Trichopteran Fibroins

Yukuhiro, Kenji; Sezutsu, Hideki; Yonemura, Naoyuki

doi:10.1007/978-94-007-7119-2_2

Cited by 7 publications

(10 citation statements)

References 38 publications

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“…mori cocoon contains two kinds of structural proteins, silk fibroin (SF) and silk sericin (SS). The SF consists of a heavy chain, light chain, and P25 in a molar ratio of 6:6:1. − The heavy and light chains are linked by a disulfide bond. The amino acid composition of the heavy chain, occupying most of the SF, is dominated by Gly (46%), Ala (30%), Ser (12%), Tyr (5.3%), and Val (1.8%) .…”

Section: Introductionmentioning

confidence: 99%

Lamellar Structure in Alanine–Glycine Copolypeptides Studied by Solid-State NMR Spectroscopy: A Model for the Crystalline Domain of Bombyx mori Silk Fibroin in Silk II Form

et al. 2020

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Bombyx mori silk fibroin (SF) fibers with excellent mechanical properties have attracted widespread attention as new biomaterials. However, the structural details are still not conclusive. Here, we propose a lamellar structure for the crystalline domain of the SF fiber based on structural analyses of the Ala Cβ peaks in the 13C cross-polarization/magic angle spinning NMR spectra of (Ala–Gly) m (m = 9, 12, 15, and 25) and 13C selectively labeled (Ala–Gly)15 model peptides. Namely, three Ala Cβ peaks with relative intensities of 1:2:1 obtained by deconvolution were assigned to two kinds of β-sheet and a β-turn, which are interpreted as a lamellar structure formed by repetitive folding using β-turns every eighth amino acid, for which the basic structure is (Ala–Gly)4 in an antipolar arrangement. The dynamics and intermolecular arrangement were further studied using 13C solid-state spin–lattice relaxation time observations and the rotational echo double resonance experiments, respectively.

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Section: Introductionmentioning

confidence: 99%

Lamellar Structure in Alanine–Glycine Copolypeptides Studied by Solid-State NMR Spectroscopy: A Model for the Crystalline Domain of Bombyx mori Silk Fibroin in Silk II Form

et al. 2020

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“…The amino acid composition of the heavy chain that comprises most of SF [10][11][12] is Gly (46 %), Ala (30 %), Ser (12 %), Tyr (5.3 %) and Val (1.8 %). In addition to the fundamental motif (GA)m, the presence of characteristic repeat sequences within the heavy chain was reported by Zhou et al [13,14].…”

Section: Introductionmentioning

confidence: 99%

Chain-folded lamellar structure and dynamics of the crystalline fraction of Bombyx mori silk fibroin and of (Ala-Gly-Ser-Gly-Ala-Gly)n model peptides

Asakura

Ogawa

Naito

et al. 2020

International Journal of Biological Macromolecules

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“…Silks continue to attract the attention of researchers in biology, biochemistry, biophysics, analytical chemistry, polymer technology, textile technology, and tissue engineering because of their supreme physical and medical properties …”

Section: Introductionmentioning

confidence: 99%

Local Structure and Dynamics of Serine in the Heterogeneous Structure of the Crystalline Domain of Bombyx mori Silk Fibroin in Silk II Form Studied by 2D ¹³C–¹³C Homonuclear Correlation NMR and Relaxation Time Observation

et al. 2014

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The crystalline fraction (Cp fraction) of silk fibroin in silk II form from the silkworm Bombyx mori is the classic example of antiparallel β-sheet and consists mainly of Ala, Ser, and Gly. In the 13C CP/MAS NMR spectrum, the Ala Cβ, Ser Cα, and Ser Cβ peaks are asymmetric, showing the heterogeneous nature of the structure, which is shown to consist of two different packing geometries, denoted domains A and B. In this work, these peaks were resolved and assigned using 2D 13C–13C homonuclear correlation NMR spectra collected with different dipolar- assisted rotational resonance (DARR) mixing times. The local structure and dynamics of serine in the Cp fraction are discussed in detail. Model peptides of the Cp fraction, [3-13C]Ser-(AGSGAG)5 with different [3-13C]Ser labeling positions, were prepared to clarify that the individual peaks of the Ser Cβ carbons come from different domains, not from different positions within a chain. The dynamics of these individual peaks were studied by measuring 13C T 1 values, which provide information on serine side chain dynamics and thus on the formation of intermolecular hydrogen bonding through the Ser OH group. Moreover, cross peaks between domains A and B were observed in the Ala Cβ DARR spectrum with a long mixing time of 400 ms, indicating a close contact between the two geometries. We conclude that the crystalline region is heterogeneous, comprising two closely associated packing geometries that form separate but small domains.

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Evolutionary Divergence of Lepidopteran and Trichopteran Fibroins

Cited by 7 publications

References 38 publications

Lamellar Structure in Alanine–Glycine Copolypeptides Studied by Solid-State NMR Spectroscopy: A Model for the Crystalline Domain of Bombyx mori Silk Fibroin in Silk II Form

Lamellar Structure in Alanine–Glycine Copolypeptides Studied by Solid-State NMR Spectroscopy: A Model for the Crystalline Domain of Bombyx mori Silk Fibroin in Silk II Form

Chain-folded lamellar structure and dynamics of the crystalline fraction of Bombyx mori silk fibroin and of (Ala-Gly-Ser-Gly-Ala-Gly)n model peptides

Local Structure and Dynamics of Serine in the Heterogeneous Structure of the Crystalline Domain of Bombyx mori Silk Fibroin in Silk II Form Studied by 2D ¹³C–¹³C Homonuclear Correlation NMR and Relaxation Time Observation

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Evolutionary Divergence of Lepidopteran and Trichopteran Fibroins

Cited by 7 publications

References 38 publications

Lamellar Structure in Alanine–Glycine Copolypeptides Studied by Solid-State NMR Spectroscopy: A Model for the Crystalline Domain of Bombyx mori Silk Fibroin in Silk II Form

Lamellar Structure in Alanine–Glycine Copolypeptides Studied by Solid-State NMR Spectroscopy: A Model for the Crystalline Domain of Bombyx mori Silk Fibroin in Silk II Form

Chain-folded lamellar structure and dynamics of the crystalline fraction of Bombyx mori silk fibroin and of (Ala-Gly-Ser-Gly-Ala-Gly)n model peptides

Local Structure and Dynamics of Serine in the Heterogeneous Structure of the Crystalline Domain of Bombyx mori Silk Fibroin in Silk II Form Studied by 2D 13C–13C Homonuclear Correlation NMR and Relaxation Time Observation

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Local Structure and Dynamics of Serine in the Heterogeneous Structure of the Crystalline Domain of Bombyx mori Silk Fibroin in Silk II Form Studied by 2D ¹³C–¹³C Homonuclear Correlation NMR and Relaxation Time Observation