Two distinct beta-sheet fibrils from silk protein.
This study showed that Bombyx mori silk protein could be selectively induced to fold into fibrils dominated by either cross- or parallel-beta-sheet structure, where the beta-strands arrange perpendicular or parallel to the long fibril axis, incubated in ethanol-water quiescently or in water under shear.
Gong
Zuguang
Z
Key Laboratory of Molecular Engineering of Polymers of Ministry of Education, Department of Macromolecular Science, Fudan University, 220 Handan Road, Shanghai 200433, People's Republic of China.
Huang
Lei
L
Yang
Yuhong
Y
Chen
Xin
X
Shao
Zhengzhong
Z
D000595:Amino Acid Sequence; D000818:Animals; D012831:Bombyx / Q000737:chemistry; D018360:Crystallography, X-Ray; D005349:Fibroins / Q000737:chemistry*; D008969:Molecular Sequence Data; D057139:Nanofibers / Q000737:chemistry / Q000648:ultrastructure; D017433:Protein Structure, Secondary; D047011:Silk / Q000737:chemistry*; D013050:Spectrometry, Fluorescence
D047011:Silk; D005349:Fibroins