REML estimation for binary data in GLMMs

The restricted maximum likelihood (REML) procedure is useful for inferences about variance components in mixed linear models. However, its extension to hierarchical generalized linear models (HGLMs) is often hampered by analytically intractable integrals. Numerical integration such as Gauss-Hermite quadrature (GHQ) is generally not recommended when the dimensionality of the integral is high. With binary data various extensions of the REML method have been suggested, but they have had unsatisfactory biases in estimation. In this paper we propose a statistically and computationally efficient REML procedure for the analysis of binary data, which is applicable over a wide class of models and design structures. We propose a bias-correction method for models such as binary matched pairs and discuss how the REML estimating equations for mixed linear models can be modified to implement more general models.     

A Lagrangean heuristic algorithm for disassembly scheduling with capacity constraints

This paper considers the problem of determining the disassembly schedule (quantity and timing) of products in order to satisfy the demand of their parts or components over a finite planning horizon. The objective is to minimize the sum of set-up, disassembly operation, and inventory holding costs. As an extension of the uncapacitated versions of the problem, we consider the resource capacity restrictions over the planning horizon. An integer program is suggested to describe the problem mathematically, and to solve the problem, a heuristic is developed using a Lagrangean relaxation technique together with a method to find a good feasible solution while considering the trade-offs among different costs. The effectiveness of the algorithm is tested on a number of randomly generated problems and the test results show that the heuristic suggested in this paper can give near optimal solutions within a short amount of computation time.     

Influence of protein concentration and order of addition on thermal stability of beta-lactoglobulin stabilized n-hexadecane oil-in-water emulsions at neutral pH

The influence of protein concentration and order of addition relative to homogenization (before or after) on the extent of droplet flocculation in heat-treated oil-in-water emulsions stabilized by a globular protein were examined using laser diffraction. n-Hexadecane (10 wt%) oil-in-water emulsions (pH 7, 150 mM NaCl) stabilized by beta-lactoglobulin (beta-Lg) were prepared by three methods: (1) 4 mg/mL beta-Lg added before homogenization; (2) 4 mg/mL beta-Lg added before homogenization and 6 mg/mL beta-Lg added after homogenization; (3) 10 mg/mL beta-Lg added before homogenization. The emulsions were then subjected to various isothermal heat treatments (30-95 degrees C for 20 min), with the 150 mM NaCl being added either before or after heating. Emulsion 1 contained little nonadsorbed protein and exhibited extensive droplet aggregation at all temperatures, which was attributed to the fact that the droplets had a high surface hydrophobicity, e.g., due to exposed oil or extensive protein surface denaturation. Emulsions 2 and 3 contained a significant fraction of nonadsorbed beta-Lg. When the NaCl was added before heating, these emulsions were relatively stable to droplet flocculation below a critical holding temperature (75 and 60 degrees C, respectively) but showed extensive flocculation above this temperature. The stability at low temperatures was attributed to the droplets having a relatively low surface hydrophobicity, e.g., due to complete saturation of the droplet surface with protein or due to more limited surface denaturation. The instability at high temperatures was attributed to thermal denaturation of the adsorbed and nonadsorbed proteins leading to increased hydrophobic interactions between droplets. When the salt was added to Emulsions 2 and 3 after heating, little droplet flocculation was observed at high temperatures, which was attributed to the dominance of intra-membrane over inter-membrane protein-protein interactions. Our data suggests that protein concentration and order of addition have a strong influence on the flocculation stability of protein-stabilized emulsions, which has important implications for the formulation and production of many emulsion-based products.     

Synthesis and crystal structures of novel calix[4]azacrowns

A series of novel 1,3‐altemate calix[4]arene azacrowns having mono and bis crown ethers on the lower rim of the calix[4]arene framework were synthesized. Solid‐state structures confirmed the three dimensional conformation of compounds 1–3.     

Energy level alignment at metal-octaethylporphyrin interfaces

We studied the electronic structure of copper-octaethylporphyrin (CuEOP) adsorbed on three metal surfaces--Ag(001), Ag(111), and Cu(111)--by means of ultraviolet photoelectron spectroscopy (UPS). The adsorption-induced work function shifts saturate roughly beyond two monolayers. The saturation values are substrate dependent, negative, and range from -1.30 to -0.85 eV. This shift is larger than that for tetraphenylporphyrins. The two highest occupied molecular orbitals (HOMO and HOMO-1) of the organic are clearly resolved in the UPS spectra. The origin of the negative work function shift is discussed.