针对股价预测中存在的不确定性、间断性、随机性和非线性等问题,提出一种TRSSA-ELM(Tent Random Walk Sparrow Optimization Algorithm-Extreme Learning Machine)股价预测模型。首先,采用自适应Tent混沌映射和随机游走策略对算法进行改...针对股价预测中存在的不确定性、间断性、随机性和非线性等问题,提出一种TRSSA-ELM(Tent Random Walk Sparrow Optimization Algorithm-Extreme Learning Machine)股价预测模型。首先,采用自适应Tent混沌映射和随机游走策略对算法进行改进,增强种群多样性和随机性,提高算法局部和全局的寻优能力。其次,使用单峰、多峰和固定维多峰测试函数对TRSSA(Tent Random Walk Sparrow Optimization Algorithm)性能进行了验证,相比于SSA(Sparrow Optimization Algorithm)、AO(Aquila Optimizer)、POA(Pelican Optimization Algorithm)和GWO(Grey Wolf Optimizer),TRSSA算法具有更好的收敛速度、精度和统计性质。最后,由于ELM(Extreme Learning Machine)模型随机生成权重和阈值,降低了预测精度和泛化能力,应用TRSSA算法优化ELM模型的权重和阈值,并用三安光电股票数据集对TRSSA-ELM模型进行了测试。实验结果表明,TRSSA-ELM模型相比于SSA-ELM、ELM、SVR(Support Vector Regression)和GBDT(Gradient Boosting Decision Tree),具有更好的预测精度和稳定性。展开更多
One of the difficulties in creating a blood substitute on the basis of human haemoglobin(Hb) is the toxic nature of Hb when it is outside the safe environment of the red blood cells.The plasma protein haptoglobin(Hp) ...One of the difficulties in creating a blood substitute on the basis of human haemoglobin(Hb) is the toxic nature of Hb when it is outside the safe environment of the red blood cells.The plasma protein haptoglobin(Hp) takes care of the Hb physiologically leaked into the plasma-it binds Hb and makes it much less toxic while retaining the Hb’s high oxygen transporting capacity.We used Electron Paramagnetic Resonance(EPR) spectroscopy to show that the protein bound radical induced by H2O2 in Hb and Hp-Hb complex is formed on the same tyrosine residue(s),but,in the complex,the radical is found in a more hydrophobic environment and decays slower than in unbound Hb,thus mitigating its oxidative capacity.The data obtained in this study might set new directions in engineering blood substitutes for transfusion that would have the oxygen transporting efficiency typical of Hb,but which would be non-toxic.展开更多
基金supported by the Biomedical EPR Facility of the University of Essexgranted by the EPSRC funded UK National Service for Computational Chemistry Software(NSCCS,1996-2017)Imperial College London。
文摘One of the difficulties in creating a blood substitute on the basis of human haemoglobin(Hb) is the toxic nature of Hb when it is outside the safe environment of the red blood cells.The plasma protein haptoglobin(Hp) takes care of the Hb physiologically leaked into the plasma-it binds Hb and makes it much less toxic while retaining the Hb’s high oxygen transporting capacity.We used Electron Paramagnetic Resonance(EPR) spectroscopy to show that the protein bound radical induced by H2O2 in Hb and Hp-Hb complex is formed on the same tyrosine residue(s),but,in the complex,the radical is found in a more hydrophobic environment and decays slower than in unbound Hb,thus mitigating its oxidative capacity.The data obtained in this study might set new directions in engineering blood substitutes for transfusion that would have the oxygen transporting efficiency typical of Hb,but which would be non-toxic.
