Coordination and Miss-Coordination in Market Entry Games with an Application to Congestion Externalities

Marketing,

The Coordination and Design of Point-Nonpoint Trading Programs and Agri-Environmental Policies

Agricultural agencies have long offered agri-environmental payments that are inadequate to achieve water quality goals, and many state water quality agencies are considering point-nonpoint trading to achieve the needed pollution reductions. This analysis considers both targeted and nontargeted agrienvironmental payment schemes, along with a trading program which is not spatially targeted. The degree of improved performance among these policies is found to depend on whether the programs are coordinated or not, whether double-dipping (i.e., when farmers are paid twice-once by each program-to undertake particular pollution control actions) is allowed, and whether the agri-environmental payments are targeted. Under coordination, efficiency gains only occur with double-dipping, so that both programs jointly influence farmers' marginal decisions. Without coordination, doubledipping may increase or decrease efficiency, depending on how the agri-environmental policy is targeted. Finally, double-dipping may not solely benefit farmers, but can result in a transfer of agricultural subsidies to point sources.Environmental Economics and Policy,

Improving the Efficiency and Effectiveness of Agri-environmental Policies for the Chesapeake Bay

Water Quality, Nonpoint Source Pollution, Policy Instrument, Chesapeake Bay, Environmental Economics and Policy, Resource /Energy Economics and Policy, Q25, Q58,

Multi-Market Trading for Cooperative Resource Management: An Application to Water Pollution and Fisheries

Increasingly, environmental problems are recognized to involve linkages across multiple environmental variables (e.g., pollution and a fishery). Prior work on managing these complex, linked systems generally focuses on efficiency rather than implementation. However, implementation is important and will generally involve changing human behaviors within the multiple economic sectors that impact upon the multiple environmental variables. Tradable permit markets are generally seen as a coordinating mechanism, within a particular regulated sector, that enhances efficiency by incentivizing agents to respond to behavioral choices of others within the sector. However, prior work stops short of coordinating behaviors across multiple sectors for cases where society benefits from regulation in both sectors and one sector harms the other. We analyze a multi-sector permit market involving both the externality-generating sector and the affected sector. This multi-sector market provides a mechanism for agents in one sector to respond to environmental behaviors made within the other sector. Moreover, unlike traditional permit markets in which the regulated externality sector incurs only costs, we show that the multi-sector market generates efficiency gains that may be redistributed using appropriate allocations of initial endowments. Accordingly, the multi-sector market may generate gains that benefit both sectors, resulting in a win-win outcome for both sectors. We use a simple example of a polluted fishery to illustrate the approach.Permit trading, fisheries, pollution, Shapley values, bioeconomics, Environmental Economics and Policy, Resource /Energy Economics and Policy,

THE DESIGN AND COMPARATIVE ECONOMIC PERFORMANCE OF ALTERNATIVE SECOND-BEST POINT/NONPOINT TRADING MARKETS

There is considerable interest in the use of pollution trading between point and nonpoint sources to improve the cost-effectiveness of water pollution control, but little literature to guide the design of trading systems involving nonpoint sources. We explore the design of two types of trading systems that would allow trading among and between point and nonpoint sources.Environmental Economics and Policy,

THE VALUE OF ECOLOGICAL AND ECONOMIC INFORMATION IN WATER QUALITY MANAGEMENT

Replaced with revised version of paper 08/25/03.Environmental Economics and Policy,

The SISO CSPI PDG standard for commercial off-the-shelf simulation package interoperability reference models

For many years discrete-event simulation has been used to analyze production and logistics problems in manufactur-ing and defense. Commercial-off-the-shelf Simulation Packages (CSPs), visual interactive modelling environ-ments such as Arena, Anylogic, Flexsim, Simul8, Witness, etc., support the development, experimentation and visua-lization of simulation models. There have been various attempts to create distributed simulations with these CSPs and their tools, some with the High Level Architecture (HLA). These are complex and it is quite difficult to assess how a set of models/CSP are actually interoperating. As the first in a series of standards aimed at standardizing how the HLA is used to support CSP distributed simula-tions, the Simulation Interoperability Standards Organiza-tion’s (SISO) CSP Interoperability Product Development Group (CSPI PDG) has developed and standardized a set of Interoperability Reference Models (IRM) that are in-tended to clearly identify the interoperability capabilities of CSP distributed simulations

Thermodynamics of protein folding: a random matrix formulation

The process of protein folding from an unfolded state to a biologically active, folded conformation is governed by many parameters e.g the sequence of amino acids, intermolecular interactions, the solvent, temperature and chaperon molecules. Our study, based on random matrix modeling of the interactions, shows however that the evolution of the statistical measures e.g Gibbs free energy, heat capacity, entropy is single parametric. The information can explain the selection of specific folding pathways from an infinite number of possible ways as well as other folding characteristics observed in computer simulation studies.Comment: 21 Pages, no figure

Experimental library screening demonstrates the successful application of computational protein design to large structural ensembles

The stability, activity, and solubility of a protein sequence are determined by a delicate balance of molecular interactions in a variety of conformational states. Even so, most computational protein design methods model sequences in the context of a single native conformation. Simulations that model the native state as an ensemble have been mostly neglected due to the lack of sufficiently powerful optimization algorithms for multistate design. Here, we have applied our multistate design algorithm to study the potential utility of various forms of input structural data for design. To facilitate a more thorough analysis, we developed new methods for the design and high-throughput stability determination of combinatorial mutation libraries based on protein design calculations. The application of these methods to the core design of a small model system produced many variants with improved thermodynamic stability and showed that multistate design methods can be readily applied to large structural ensembles. We found that exhaustive screening of our designed libraries helped to clarify several sources of simulation error that would have otherwise been difficult to ascertain. Interestingly, the lack of correlation between our simulated and experimentally measured stability values shows clearly that a design procedure need not reproduce experimental data exactly to achieve success. This surprising result suggests potentially fruitful directions for the improvement of computational protein design technology

The aggregation of cytochrome C may be linked to its flexibility during refolding

Large-scale expression of biopharmaceutical proteins in cellular hosts results in production of large insoluble mass aggregates. In order to generate functional product, these aggregates require further processing through refolding with denaturant, a process in itself that can result in aggregation. Using a model folding protein, cytochrome C, we show how an increase in final denaturant concentration decreases the propensity of the protein to aggregate during refolding. Using polarised fluorescence anisotropy, we show how reduced levels of aggregation can be achieved by increasing the period of time the protein remains flexible during refolding, mediated through dilution ratios. This highlights the relationship between the flexibility of a protein and its propensity to aggregate. We attribute this behaviour to the preferential urea-residue interaction, over self-association between molecules