The minimal pathway of

The minimal pathway of a stimulus-response task has the structure (con + minlinEN ET + 2 ET). 

How long does the minimal search in xlly take I have defined the minimal pathway of xlly as a truly linear pathway without any search. 

The possible representation of the memory sets (of the xl ly task) within the cerbral cortex are shown in the last two figures. The last figure shows the minimal pathway of the task xlly. 

Probably the most well-known pathway to exemplify the occurrence of complex dynamics in metabolic networks is the glycolytic pathway of yeast. Arguably one of the most modeled pathways ever, minimal models of yeast glycolysis were studied since the 1960s [94, 273, 305 308] and give rise to a rich spectrum of... 

Figure 22. The nullclines corresponding to the minimal model of glycolysis. Depending on the value of the maximal ATP utilization Vm3, the pathway either exhibits a unique steady state or allows for a bistable solution. Note that the nullcline for TP does not depend on VThe corresponding steady states are shown in Fig. 23. Parameters are Vm 3.1, K 0.57, ki 4.0, K i 0.06, and n 4 (the values do not correspond to a specific biological situation).

A further piece of evidence to elucidate the catalytic pathway of silylformylation was provided by a pair of deuterium-labeled reactions. The results revealed that the scrambling of hydrogen atoms between a hydrosilane and a terminal acetylene is minimal during the reaction and that the hydrogen atom of the formyl group and the vinylic hydrogen are derived from the hydrosilane and the acetylenic proton, respectively (Eq. 8) [15 bj. 

The role of catalysis in membrane assembly is emphasized again by the above model since the N-terminal sequence of the nascent polypeptide chain of a spanning protein is released by proteolysis as soon as it reaches the cytosol. The N-terminal polypeptide chain extension may help the chain penetrate the hydrophobic bilayer and solubilize the resulting hydrophobic N-terminal part of the chain in the aqueous medium of the cytoplasm. However, the role of the protease-catalyzed hydrolysis of the polypeptide chain in membrane assembly is minimized in the membrane trigger hypothesis (99). According to this model, the essential role of the leader sequence would be to modify, in association with the lipid bilayer, the folding pathway of the protein in such a way that the polypeptide chain could span the membrane. 

No attempt to determine the folding pathway of a protein from the denatured to the native state either by energy minimization or by molecular dynamics has yet been successful. Many people believe that it would be more effective to approach the problem through a study of the formation and interaction of secondary structural units. A conservative appraisal of the situation is that this problem is not one that can be solved by increase in computer power alone. 

The point of a transient kinetic experiment is to establish the reaction pathway by examination of the concentration dependence of the rate of reaction. It is the goal of proper data analysis to ferret out the best fit to the data to establish the reaction mechanism containing the minimal number of steps. I will describe two... 

Camacho and Thirumalai [87] investigated the effect of strong covalent interactions (disulfide bonds) on the folding pathway of a minimal lattice model. They found that the folding rate is fastest when a proper balance is achieved between effective hydrophobic interactions and the strength of disulfide bonds. This rationalizes how weak denaturing conditions can accelerate the folding process of real crosslinked proteins. 

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