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Regulation of β-Sheet Formation in Fibroin

Residues of fibroin create electrostatic repulsion

In the fibroin β-sheet there are specific residues that are preserved in the N-terminal domain in order to prevent premature sheet formation at a neutral pH. Glu98 and Asp100 are both acidic, meaning they have negative charges when at a neutral pH. Since they have the same charge, the residues will create electrostatic repulsion which can cause the side chains to repel each other. At a low pH however, these residues would become protonated and lose their charge. When the charge repulsion is not present, hydrogen bonding and hydrophobic interactions become the main driving force of β-sheet formation. Therefore, when at a neutral pH Glu98 and Asp100 are deprotonated, and the electrostatic repulsion occurs. This repulsion reduces structural stability or can even prevent premature formation of the β-sheet. By preventing the premature formation, the electrostatic repulsions help ensure that the β-sheet is formed correctly which will allow for fibroin to function properly. The regulation of the β-sheet formation is especially important to the integrity of silk since fibroin is one of the primary structural proteins in silk.[1]

  1. ^ He, Yong-Xing; Zhang, Nan-Nan; Li, Wei-Fang; Jia, Ning; Chen, Bao-Yu; Zhou, Kang; Zhang, Jiahai; Chen, Yuxing; Zhou, Cong-Zhao (February 23, 2012). "N-Terminal Domain of Bombyx mori Fibroin Mediates the Assembly of Silk in Response to pH Decrease". Journal of Molecular Biology. 418: 197–207 – via Elsevier Science Direct. {{cite journal}}: line feed character in |title= at position 50 (help)

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