An investigation of the structure of silk fibroin.

Abstract An investigation based on new X-ray diffraction data, including quantitative spectrometric measurements of X-ray intensities, has led to the derivation of the fundamental structural features of silk fibroin. The structure consists of extended polypeptide chains bonded together by lateral N—H…O hydrogen bonds to form antiparallel-chain pleated sheets. The sequence-G-X-G-X-G-X-in which G represents glycyl and X alanyl or seryl residues predominates throughout the structure, so that adjacent sheets pack together at distances of about 3.5 and 5.7 A. Longer inter-sheet distances are explained by the presence in the structure of the larger amino-acid residues, such as tyrosine.

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