We present the design of micro-helix metamaterial supporting high sound absorption characteristic by 3D printing. The sample structure which is fabricated out of polylactide （PLA） material, many micro-helix are arra...We present the design of micro-helix metamaterial supporting high sound absorption characteristic by 3D printing. The sample structure which is fabricated out of polylactide （PLA） material, many micro-helix are arranged by periodic arrays on XY plane. Experiment measurement results show that different geometrical dimensions of helix vestibule and cavity depth have a great effect on sound absorption coefficient. Physical mechanism depends on the friction and viscosity between the air and the helix vestibule. This work shows great potential of micro-structure metamaterial in noise control applications require light weight and large rigid of sound absorption.展开更多
The conformational transformation of a 30-residue peptide H（Ala-Gly-Ser-Gly-AIa-Gly）5OH, i.e., （AGSGAG）5, extracted from highly crystalline region of Bombyx mori （B. mori） silk fibroin was described by using the...The conformational transformation of a 30-residue peptide H（Ala-Gly-Ser-Gly-AIa-Gly）5OH, i.e., （AGSGAG）5, extracted from highly crystalline region of Bombyx mori （B. mori） silk fibroin was described by using the high resolution solid state 13^C NMR, and CD spectroscopies. Based on the conformation-dependent 13^C NMR chemical shifts of the Ala, Gly and Ser residues and the line-shape analysis of the conformation sensitive Ala Cβ resonance, the peptide revealed a strong preference for silk Ⅱ structural form, i,e,, an antiparallel fl-sheet structure （φ= - 140±20°and ψ= 135±20°） in solid state. On the contrary, the CD spectra of this peptide in the two non-native hexafluorinated fibre spinning solvents, hexafluoroisopropanol （HFIP） and hexafluoroacetone （HFA）, exhibited the existence of an unusual tightly-folded conformation resembling 310-helix （φ=- 60±20° and ψ=-30±20°）, as judged from the R ratio of [θ]222/[θ]203 in HFIP solution, whereas a dynamically averaged unordered structure in HFA, Taken together, the information inclined to hypothesis that the primary structure of the highly crystalline regions of B. mori silk fibroin may be easily accessible to the large conformational changes, which in turn may be critical for facilitating the structural transformation from unprocessed silk fibroin （silk I form） to processed silk fiber （silk Ⅱform）.展开更多
基金supported by the National Natural Science Foundation of China (11704314 and 11474230)the Fundamental Research Funds for the Central Universities (3102016QD056) for financial support
文摘We present the design of micro-helix metamaterial supporting high sound absorption characteristic by 3D printing. The sample structure which is fabricated out of polylactide （PLA） material, many micro-helix are arranged by periodic arrays on XY plane. Experiment measurement results show that different geometrical dimensions of helix vestibule and cavity depth have a great effect on sound absorption coefficient. Physical mechanism depends on the friction and viscosity between the air and the helix vestibule. This work shows great potential of micro-structure metamaterial in noise control applications require light weight and large rigid of sound absorption.
基金Project supported by the National Natural Science Foundation of China （No. 20404011） and Zhejiang Natural Science Foundation of China （No. R404066）.
文摘The conformational transformation of a 30-residue peptide H（Ala-Gly-Ser-Gly-AIa-Gly）5OH, i.e., （AGSGAG）5, extracted from highly crystalline region of Bombyx mori （B. mori） silk fibroin was described by using the high resolution solid state 13^C NMR, and CD spectroscopies. Based on the conformation-dependent 13^C NMR chemical shifts of the Ala, Gly and Ser residues and the line-shape analysis of the conformation sensitive Ala Cβ resonance, the peptide revealed a strong preference for silk Ⅱ structural form, i,e,, an antiparallel fl-sheet structure （φ= - 140±20°and ψ= 135±20°） in solid state. On the contrary, the CD spectra of this peptide in the two non-native hexafluorinated fibre spinning solvents, hexafluoroisopropanol （HFIP） and hexafluoroacetone （HFA）, exhibited the existence of an unusual tightly-folded conformation resembling 310-helix （φ=- 60±20° and ψ=-30±20°）, as judged from the R ratio of [θ]222/[θ]203 in HFIP solution, whereas a dynamically averaged unordered structure in HFA, Taken together, the information inclined to hypothesis that the primary structure of the highly crystalline regions of B. mori silk fibroin may be easily accessible to the large conformational changes, which in turn may be critical for facilitating the structural transformation from unprocessed silk fibroin （silk I form） to processed silk fiber （silk Ⅱform）.
