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Policy Points Looking for a way to curtail market power abuses in health care and rein in prices, 20 states have restricted most-favored-nation (MFN) clauses in some health care contracts. Little is known as to whether restrictions on MFN clauses slow health care price growth. Banning MFN clauses between insurers and hospitals in highly concentrated insurer markets seems to improve competition and lead to lower hospital prices.ContextMost-favored-nation (MFN) contract clauses have recently garnered attention from both Congress and state legislatures looking for ways to curtail market power abuses in health care and rein in prices. In health care, a typical MFN contract clause is stipulated by the insurer and requires a health care provider to grant the insurer the lowest (i.e., the most-favored) price among the insurers it contracts with. As of August 2020, 20 states restrict the use of MFN clauses in health care contracts (19 states ban their use in at least some health care contracts), with 8 states prohibiting their use between 2010 and 2016.MethodsUsing event study and difference-in-differences research designs, we compared prices for a standardized hospital admission in states that banned MFN clauses between 2010 and 2016 with standardized hospital admission prices in states without MFN bans.FindingsOur results show that bans on MFN clauses reduced hospital price growth in metropolitan statistical areas (MSAs) with highly concentrated insurer markets. Specifically, we found that mean hospital prices in MSAs with highly concentrated insurer markets would have been $472 (2.8%) lower in 2016 had the MSAs been in states that banned MFN clauses in 2010. In 2016, the population in our sample that resided in MSAs with highly concentrated insurer markets was just under 75 million (23% of the US population). Hence, banning MFN clauses in all MSAs in our sample with highly concentrated insurer markets in 2010 would have generated savings on hospital expenditures in the range of $2.4 billion per year.ConclusionsOur empirical findings suggest banning MFN clauses between insurers and providers in highly concentrated insurer markets would improve competition and lead to lower prices and expenditures.

This paper describes the fabrication of a fluidic device for detecting and separating diamagnetic materials that differ in density. The basis for the separation is the balance of the magnetic and gravitational forces on diamagnetic materials suspended in a paramagnetic medium. The paper demonstrates two applications of separations involving particles suspended in static fluids for detecting the following: (i) the binding of streptavidin to solid-supported biotin and (ii) the binding of citrate-capped gold nanoparticles to amine-modified polystyrene spheres. The paper also demonstrates a microfluidic device in which polystyrene particles that differ in their content of C[H.sub.2]Cl groups are continuously separated and collected in a flowing stream of an aqueous solution of Gd[Cl.sub.3]. The procedures for separation and detection described in this paper require only gadolinium salts, two NdFeB magnets, and simple microfluidic devices fabricated from poly(dimethylsiloxane). This device requires no power, has no moving parts, and may be suitable for use in resource-poor environments.

A study was carried to investigate the role of electrostatics in the interaction of a protein and sodium dodecyl sulfate (SDS) using native carbonic anhydrase (BCA) and its charged-modified derivative (BCA-Ac(sub 18)) having all the lysine groups acetylated. It was believed that if the derivative differs from the native protein in charge then proteins and their derivatives might behave differently toward SDS.

This paper uses capillary electrophoresis to follow a globular metalloprotein--bovine carbonic anhydrase II (BCA, EC 4.2.1.1)--on unfolding upon treatment with sodium dodecyl sulfate (SDS) and refolding upon removal of SDS, both in the presence and the absence of its Zn(II) cofactor. This research demonstrates that the Zn(II) cofactor is not required for refolding into a nativelike conformation, does not remain associated with the unfolded protein, and does not significantly change the rate of refolding. The presence of the Zn(II) cofactor, however, does increase the total amount of recovered protein by a factor of 2. Capillary electrophoresis could distinguish between native and denatured protein, based on the difference in electrophoretic mobility between the native protein and the aggregate of denatured protein and SDS. In addition, the active site was probed by observing binding of BCA to a charged arylsulfonamide using affinity capillary electrophoresis. These studies provide a foundation for future physical-organic studies using BCA as a model to examine interactions between proteins and SDS.

The COVID-19 pandemic exposed the weaknesses of the U.S. health care system's reliance on private, employer-based health insurance. The crisis in health care access and affordability has increased support for a public option--the choice to purchase a state-initiated health plan with publicly determined rates. Congressional gridlock, however, may dim the chances for a federal public option. States have stepped into the policy vacuum, proposing forty-nine bills to establish state public options since 2010, including three that became law. This article provides a comprehensive survey and taxonomy of state public option proposals from 2010-2021, identifying three main models: (1) Medicaid Buy-In Public Options; (2) Marketplace-Based Public Options; and (3) Comprehensive Public Options. Though each model serves different policy goals and varies in scope, the defining aim of all public option plans is to improve access to affordable health coverage by applying public payment rates to the private insurance market. We seek to answer whether state public option plans are legally viable and "worth it" for states to pursue. The answer is yes to both, but, surprisingly, the degree of legal difficulty is inversely related to the scope of the plan's reach--the broadest plans have fewer legal hurdles than narrower plans. Moreover, the policy effects increase with the scope of the plan and the robustness of the controls on provider payment rates. Public options with modest provider rate controls may have too little impact on affordability and costs, falling short of their defining goal of improving affordability. As a result, the legal and political difficulty of enacting such plans may not be worth it. State public option plans may be most effective when they cover a broad swath of the population and pursue robust provider rate controls. In short, for state public option plans to be worth it, bigger is better. [ABSTRACT FROM AUTHOR]

A study is conducted that compares the folding of two polypeptides, bovine carbonic anhydrase (BCA) and peracetylated BCA having the same sequence of amino acids but differing by 18 formal units of charge, from a solution containing denaturing concentrations of sodium dodecyl sulphate. The study suggests that large differences in the net charge of polypeptide have no significant influence on the structure, ability to refold or its rate.

This study compares the folding of two polypeptides-bovine carbonic anhydrase (BCA) and peracetylated BCA (BCA-Ac18)--having the same sequence of amino acids but differing by 18 formal units of charge, from a solution containing denaturing concentrations of sodium dodecyl sulfate (SDS). Acetylation of BCA with acetic anhydride converts all 18 lysine-€-NH3+ groups to lysine-€-NHCOCH3 groups and generates BCA-Ac18. Both BCA and BCA-Ac18 are catalytically active, and circular dichroism spectroscopy (CD) suggests that they have similar secondary and tertiary structures. SDS at concentrations above ∼10 mM denatured both proteins. When the SDS was removed by dialysis, both proteins were regenerated in native form. This study suggests that large differences in the net charge of the polypeptide have no significant influence on the structure, the ability to refold, or the rate of refolding of this protein from solutions containing SDS. This study reinforces the idea that charged residues on the surface of BCA do not guide protein folding and raises the broader question of why proteins have charged residues on their surface, outside of the region of the active site. [ABSTRACT FROM AUTHOR]

The article reports on the use of carbonic anhydrase in the study of protein-ligand binding. The protein carbonic anhydrase can be used as a model in the study of biophysics and medical chemistry because of its properties. In the study of protein-ligand binding, the use of carbonic anhydrase as a model is ideal because of its single-chain structure, weight, and availability. The article provides an overview of the use of carbonic anhydrase as a model in biophysics.