title: Two distinct beta-sheet fibrils from silk protein.
abstract: 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.
authors.affiliation: 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.
authors.forename: Zuguang
authors.initials: Z
authors.lastname: Gong
authors.forename: Lei
authors.initials: L
authors.lastname: Huang
authors.forename: Yuhong
authors.initials: Y
authors.lastname: Yang
authors.forename: Xin
authors.initials: X
authors.lastname: Chen
authors.forename: Zhengzhong
authors.initials: Z
authors.lastname: Shao
mesh_terms: 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
chemical_list: D047011:Silk; D005349:Fibroins