The effect of cooling rate on the transition of dendrite morphology of a Mg-6Gd （wt%） alloy was semiquantitatively analyzed under a constant temperature gradient by using synchrotron X-ray radiographic technique. Re...The effect of cooling rate on the transition of dendrite morphology of a Mg-6Gd （wt%） alloy was semiquantitatively analyzed under a constant temperature gradient by using synchrotron X-ray radiographic technique. Results show that equiaxed dendrites, including exotic ＇butterfly-shaped＇ dendrite morphology, dominate at high cooling rate （〉1 K/s）. When the cooling rate decreases in the range of 0.5-1 K/s, the equiaxed-to-columnar transition takes place, and solute segregates at the center of two long dendrite arms （LDA） of the ＇butterfly-shaped＇ dendrite. When the cooling rate is lower than 0.3 K/s, directional solidification occurs and the columnar dendritic growth direction gradually rotates from the crystalline axis to the thermal gradient direction with an increase in cooling rate. Meanwhile, interface moves faster but the dendrite arm spacing decreases. Floating, collision and rotation of dendrites under convection were also studied in this work.2018 Published by Elsevier Ltd on behalf of The editorial office of Journal of Materials Science ＆ Technology.展开更多
Limited digestion of fructose 1,6-bisphosphatase with subtilisin produces an S-peptide with an about 60-residue peptide fragment that is non-covalently associated with the enzyme. The 60-residue peptide fragment con-s...Limited digestion of fructose 1,6-bisphosphatase with subtilisin produces an S-peptide with an about 60-residue peptide fragment that is non-covalently associated with the enzyme. The 60-residue peptide fragment con-sists of the most part of allosteric site for AMP binding. It could be separated from S-protein by gel filtration with a Sephadex G-75 column equilibrated with 9% formic acid. According to X-ray diffraction results the S-peptide consists of two α-helices without β-strand and the α-helix content is about 60% in the 60-residue-peptide fragment. When the enzyme is subjected to limited proteolysis with subtilisin, the secondary structure of the enzyme does not show a de-tectable change in CD spectrum. The CD spectra of the isolated S-peptide were measured under different concentra-tions. In the absence of GuHCl, S-peptide had 30% a-helix and 38.5% turn-like structure but had no β-strand, sug-gesting that the N-terminal 60-residue fragment, which is synthesized initially by ribosome, would form a conforma-tion spontaneously similar to that of the isolated 60-residue-peptide, i.e. about 30% a-helix and 30% turn-like struc-ture. As the elongation of the peptide chain of the enzyme proceeds, the newly synthesized segment or the final entire enzyme, in turn, affects the conformation of prior peptide segment and adjusts its conformation to the final native state. The content of a-helix did not increase as perturbing the conformation of S-peptide by adding ethanol, cyclohex-ane or a small amount of SDS. On the contrary, the ordered structure was slightly decreased, indicating that the dif-ference of conformations of S-peptide in the isolated form and in the associated protein was not an artifact produced by isolation process.展开更多
基金financially supported by the Program of Shanghai Subject Chief Engineering (No. 14XD1425000)the National Natural Science Foundation of China (No. 51304135)the Chinese Scholarship Council and DOE (No. DE-FG02-07ER46417)
文摘The effect of cooling rate on the transition of dendrite morphology of a Mg-6Gd （wt%） alloy was semiquantitatively analyzed under a constant temperature gradient by using synchrotron X-ray radiographic technique. Results show that equiaxed dendrites, including exotic ＇butterfly-shaped＇ dendrite morphology, dominate at high cooling rate （〉1 K/s）. When the cooling rate decreases in the range of 0.5-1 K/s, the equiaxed-to-columnar transition takes place, and solute segregates at the center of two long dendrite arms （LDA） of the ＇butterfly-shaped＇ dendrite. When the cooling rate is lower than 0.3 K/s, directional solidification occurs and the columnar dendritic growth direction gradually rotates from the crystalline axis to the thermal gradient direction with an increase in cooling rate. Meanwhile, interface moves faster but the dendrite arm spacing decreases. Floating, collision and rotation of dendrites under convection were also studied in this work.2018 Published by Elsevier Ltd on behalf of The editorial office of Journal of Materials Science ＆ Technology.
基金Project supported in part by the National Natural Science Foundation of China and the Climbing Project of the State Science and Technology Commission of China.
文摘Limited digestion of fructose 1,6-bisphosphatase with subtilisin produces an S-peptide with an about 60-residue peptide fragment that is non-covalently associated with the enzyme. The 60-residue peptide fragment con-sists of the most part of allosteric site for AMP binding. It could be separated from S-protein by gel filtration with a Sephadex G-75 column equilibrated with 9% formic acid. According to X-ray diffraction results the S-peptide consists of two α-helices without β-strand and the α-helix content is about 60% in the 60-residue-peptide fragment. When the enzyme is subjected to limited proteolysis with subtilisin, the secondary structure of the enzyme does not show a de-tectable change in CD spectrum. The CD spectra of the isolated S-peptide were measured under different concentra-tions. In the absence of GuHCl, S-peptide had 30% a-helix and 38.5% turn-like structure but had no β-strand, sug-gesting that the N-terminal 60-residue fragment, which is synthesized initially by ribosome, would form a conforma-tion spontaneously similar to that of the isolated 60-residue-peptide, i.e. about 30% a-helix and 30% turn-like struc-ture. As the elongation of the peptide chain of the enzyme proceeds, the newly synthesized segment or the final entire enzyme, in turn, affects the conformation of prior peptide segment and adjusts its conformation to the final native state. The content of a-helix did not increase as perturbing the conformation of S-peptide by adding ethanol, cyclohex-ane or a small amount of SDS. On the contrary, the ordered structure was slightly decreased, indicating that the dif-ference of conformations of S-peptide in the isolated form and in the associated protein was not an artifact produced by isolation process.
