Structural study of irregular amino acid sequences in the heavy chain of Bombyx mori silk fibroin
BIOMACROMOLECULES, 6(5), 2563–2569.
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
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.
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