行走模式对人体下肢三维步态、肌电信号的影响

目的:揭示人体在主动和被动两种行走模式下的步态特征与下肢主要肌群的肌电信号变化规律。方法:选取12名在校男大学生,通过Greenjog履带式自发力跑台和h/p/cosmos电动跑台建立主动式和被动式行走模型,先后在两种模式下以3种递增速度即慢速(2 km/h)、常速(4 km/h)、和快速(6 km/h)进行一次性步行运动,运用三维运动捕捉分析系统和表面肌电测试仪,分别对每种速度采集2 min的连续三维步态和肌电信号数据。结果:慢速时,被动式行走的支撑相占比显著高于主动式行走(P<0.05),而摆动相占比和膝关节角度变化值则显著低于主动式行走(P<0.05);常速时,被动式行走的膝关节角度变化值和股二头肌积分肌电值显著低于主动式行走(P<0.05);快速时,被动式行走的膝关节、踝关节角度变化值和股二头肌积分肌电值显著低于主动式行走(P<0.01);此外,随着步行速度的增加,被动式行走的胫骨前肌积分肌电值呈现显著增高的趋势(P<0.05)。结论:随着步行速度的增加,人体主动步行时的膝关节活动范围更充分,对主动肌的锻炼作用更明显。     

The intrinsic contributions of tyrosine, serine, glycine and arginine to the affinity and specificity of antibodies

Synthetic antibody libraries with restricted chemical diversity were used to explore the intrinsic contributions of four amino acids (Tyr, Ser, Gly and Arg) to the affinity and specificity of antigen recognition. There was no correlation between nonspecific binding and the content of Tyr, Ser or Gly in the antigen-binding site, and in fact, the most specific antibodies were those with the highest Tyr content. In contrast, Arg content was clearly correlated with increased nonspecific binding. We combined Tyr, Ser and Gly to generate highly specific synthetic antibodies with affinities in the subnanomolar range, showing that the high abundance of Tyr, Ser and Gly in natural antibody germ line sequences reflects the intrinsic capacity of these residues to work together to mediate antigen recognition. Despite being a major functional contributor to co-evolved protein-protein interfaces, we find that Arg does not contribute generally to the affinity of naïve antigen-binding sites and is detrimental to specificity. Again, this is consistent with studies of natural antibodies, which have shown that nonspecific, self-reactive antibodies are rich in Arg and other positively charged residues. Our findings suggest that the principles governing naïve molecular recognition differ from those governing co-evolved interactions. Analogous studies can be designed to explore the roles of the other amino acids in molecular recognition. Results of such studies should illuminate the basic principles underlying natural protein-protein interactions and should aid the design of synthetic binding proteins with functions beyond the scope of natural proteins.