This article deals with the reflective function of the differential systems. The results are applied to discussion of the existence and stability of the periodic solutions of these systems.
In order to establish the sufficient and necessary condition that arbitrarily reliable systems can not be constructed with function elements under interference sources, it is very important to expand set of interferen...In order to establish the sufficient and necessary condition that arbitrarily reliable systems can not be constructed with function elements under interference sources, it is very important to expand set of interference sources with the above property. In this paper, the models of two types of interference sources are raised respectively: interference source possessing real input vectors and constant reliable interference source. We study the reliability of the systems effected by the interference sources, and the lower bound of the reliability is presented. The results show that it is impossible that arbitrarily reliable systems can not be constructed with the elements effected by above interference sources.展开更多
For the design and optimization of functional peptides, unravelling the structures of individual building blocks as well as the properties of the ensemble is paramount. TI＇R1, derived from human transthyretin, is a f...For the design and optimization of functional peptides, unravelling the structures of individual building blocks as well as the properties of the ensemble is paramount. TI＇R1, derived from human transthyretin, is a fibril-forming peptide implicated in diseases such as familial amyloid polyneuropathy and senile systemic amyloidosis. The functional peptide TTR1-RGD, based on a TFR1 scaffold, was designed to specifically interact with cells. Here, we used scanning tunneling microscopy （STM） to analyze the assembly structures of TTRl-related peptides with both the reverse sequence and the modified forward sequence. The site- specific analyses show the following： i） The TIR1 peptide is involved in assembly, nearly covering the entire length within the ordered [3-sheet structures, ii） For TTR1-RGD peptide assemblies, the TTR1 motif forms the ordered [3-sheet while the RGDS motif adopts a flexible conformation allowing it to promote cell adhesion. The key site is clearly identified as the linker residue Gly13. iii） Close inspection of the forward and reverse peptide assemblies show that in spite of the difference in chemistry, they display similar assembling characteristics, illustrating the robust nature of these peptides, iv） Glycine linker residues are included in the ^-strands, which strongly suggests that the sequence could be optimized by adding more linker residues. These garnered insights into the assembled structures of these peptides help unravel the mechanism driving peptide assemblies and instruct the rational design and optimization of sequence- programmed peptide architectures.展开更多
文摘This article deals with the reflective function of the differential systems. The results are applied to discussion of the existence and stability of the periodic solutions of these systems.
基金Tsinghua University Research Foundation(JC2000025)
文摘In order to establish the sufficient and necessary condition that arbitrarily reliable systems can not be constructed with function elements under interference sources, it is very important to expand set of interference sources with the above property. In this paper, the models of two types of interference sources are raised respectively: interference source possessing real input vectors and constant reliable interference source. We study the reliability of the systems effected by the interference sources, and the lower bound of the reliability is presented. The results show that it is impossible that arbitrarily reliable systems can not be constructed with the elements effected by above interference sources.
文摘For the design and optimization of functional peptides, unravelling the structures of individual building blocks as well as the properties of the ensemble is paramount. TI＇R1, derived from human transthyretin, is a fibril-forming peptide implicated in diseases such as familial amyloid polyneuropathy and senile systemic amyloidosis. The functional peptide TTR1-RGD, based on a TFR1 scaffold, was designed to specifically interact with cells. Here, we used scanning tunneling microscopy （STM） to analyze the assembly structures of TTRl-related peptides with both the reverse sequence and the modified forward sequence. The site- specific analyses show the following： i） The TIR1 peptide is involved in assembly, nearly covering the entire length within the ordered [3-sheet structures, ii） For TTR1-RGD peptide assemblies, the TTR1 motif forms the ordered [3-sheet while the RGDS motif adopts a flexible conformation allowing it to promote cell adhesion. The key site is clearly identified as the linker residue Gly13. iii） Close inspection of the forward and reverse peptide assemblies show that in spite of the difference in chemistry, they display similar assembling characteristics, illustrating the robust nature of these peptides, iv） Glycine linker residues are included in the ^-strands, which strongly suggests that the sequence could be optimized by adding more linker residues. These garnered insights into the assembled structures of these peptides help unravel the mechanism driving peptide assemblies and instruct the rational design and optimization of sequence- programmed peptide architectures.
