2005 article

Conformational Changes Induced in Bombyx mori Silk Fibroin by Cyclodextrin Inclusion Complexation

Rusa, C. C., Bridges, C., Ha, S.-W., & Tonelli, A. E. (2005, May 27). Macromolecules.

By: C. Rusa n, C. Bridges n, S. Ha n & A. Tonelli n

topics (OpenAlex): Silk-based biomaterials and applications; biodegradable polymer synthesis and properties; Fiber-reinforced polymer composites
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Source: Web Of Science
Added: August 6, 2018

2005 article

Structural Studies of Bombyx mori Silk Fibroin during Regeneration from Solutions and Wet Fiber Spinning

Ha, S.-W., Tonelli, A. E., & Hudson, S. M. (2005, April 21). Biomacromolecules.

By: S. Ha n, A. Tonelli n & S. Hudson n

MeSH headings : Animals; Bombyx; Fibroins / analysis; Fibroins / chemical synthesis; Silk / analysis; Silk / chemical synthesis; Solutions; Technology, Pharmaceutical / methods
topics (OpenAlex): Silk-based biomaterials and applications; Silkworms and Sericulture Research; Insect and Arachnid Ecology and Behavior
TL;DR: The regenerated fibroin fibers showed much better mechanical properties compared to the native silk fiber and their physical and chemical properties were characterized by X-ray diffraction, solid state (13)C NMR spectroscopy, SinTech tensile testing, and SEM. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

2005 article

Structural Study of Irregular Amino Acid Sequences in the Heavy Chain of Bombyx mori Silk Fibroin

Ha, S.-W., Gracz, H. S., Tonelli, A. E., & Hudson, S. M. (2005, July 12). Biomacromolecules.

By: S. Ha n, H. Gracz n, A. Tonelli n & S. Hudson n

MeSH headings : Amino Acid Sequence; Amino Acids / chemistry; Animals; Bombyx; Crystallography, X-Ray; Fibroins / chemistry; Insect Proteins / chemistry; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Peptides / chemistry; Polymers / chemistry; Protein Conformation; Protein Structure, Secondary; Sequence Homology, Amino Acid; Silk / chemistry; Silk / metabolism; X-Ray Diffraction
topics (OpenAlex): Silk-based biomaterials and applications; Antimicrobial Peptides and Activities; Neurobiology and Insect Physiology Research
TL;DR: The 3-D structure determined for this peptide shows that it makes a loop structure (distorted omega shape), which implies that the preceding backbone direction is changed by 180 degrees, i.e., reversed, by this sequence, which may facilitate the beta-sheet formation between the crystal-forming building blocks, GAGAGS/GY approximately GY sequences, in the fibroin heavy chain. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

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