Abstract: The present invention relates to compositions comprising GLP-2 protein or variants thereof linked to extended recombinant polypeptide (XTEN), isolated nucleic acids encoding the compositions and vectors and host cells containing the same, and methods of making and using such compositions in the treatment of GLP-2 related conditions.

Abstract: An illustrative example embodiment of a fuel cell component includes a graphite substrate, a polytetrafluoroethylene (PTFE) layer adjacent a portion of the graphite substrate, and a plurality of segments of acrylic adhesive between the portion of the graphite substrate and the PTFE layer. The acrylic adhesive secures the PTFE layer to the portion of the graphite substrate. There is spacing between adjacent ones of the segments.

Abstract: An illustrative example embodiment of method of making a fuel cell component includes placing a graphite substrate and a polytetrafluoroethylene (PTFE) layer in a heated press with a fluoroelastomer adhesive between the graphite substrate and the PTFE layer; pressing the PTFE layer, the fluoroelastomer adhesive and the graphite substrate together using the heated press; removing the graphite substrate, the fluoroelastomer adhesive and the PTFE layer from the heated press; and allowing the graphite substrate, the fluoroelastomer adhesive, and the PTFE layer to cool.

Abstract: A multi-functional lead anti-dissolution composition based on 100 parts by weight consisting of: a succinic acid in an amount of from 30 to 70 percent by weight; and a tartaric acid in an amount of from 70 to 30 percent by weight. The composition does not include any phosphates, thereby not contributing to the phosphate footprint in the water supply. The composition includes organic acids that have anti-inflammatory properties in addition to reducing lead dissolution in drinking water.

Abstract: A multi-functional lead anti-dissolution composition based on 100 parts by weight consisting of: a succinic acid in an amount of from 30 to 70 percent by weight; and a tartaric acid in an amount of from 70 to 30 percent by weight. The composition does not include any phosphates, thereby not contributing to the phosphate footprint in the water supply. The composition includes organic acids that have anti-inflammatory properties in addition to reducing lead dissolution in drinking water.

Abstract: A profiler which spatially profiles a hydrophobicity distribution for the transmembrane protein based on a scaled hydrophobicity value, includes an identifier for identifying a residue external to a membrane and removing the residue to obtain a truncated structure comprising plural residue side-chains, and a calculator which calculates plural residue centroids for the plural residue side-chains, calculates a distribution of the plural residue centroids, and obtains a geometric center for the distribution.

Abstract: Generally, the present invention provides a number of procedures to spatially profile proteins by using hydrophobic moments. In all procedures, a hydrophobicity distribution of a protein is shifted and normalized. In one procedure, a shape or profile of a curve of a second-order moment of hydrophobicity is determined. A second procedure involves determining one or more ratios, such as the ratio of a distance at which the second order moment of hydrophobicity vanishes to the distance at which a zero-order moment of hydrophobicity vanishes. The distance at which a peak occurs in a profile of the zero- or second-order moment of hydrophobicity can also be used for comparison. For many of these procedures, a surface or profiling contour can be chosen and used to accumulate hydrophobicities and to determine the moments. These procedures can be combined to provide a good mathematical determination of whether a protein belongs to a particular class of proteins.

Abstract: Generally, the present invention provides a number of procedures to spatially profile proteins by using hydrophobic moments. In all procedures, a hydrophobicity distribution of a protein is shifted and normalized. In one procedure, a shape or profile of a curve of a second-order moment of hydrophobicity is determined. A second procedure involves determining one or more ratios, such as the ratio of a distance at which the second order moment of hydrophobicity vanishes to the distance at which a zero-order moment of hydrophobicity vanishes. The distance at which a peak occurs in a profile of the zero- or second-order moment of hydrophobicity can also be used for comparison. For many of these procedures, a surface or profiling contour can be chosen and used to accumulate hydrophobicities and to determine the moments. These procedures can be combined to provide a good mathematical determination of whether a protein belongs to a particular class of proteins.

Abstract: Techniques for analyzing protein structures, such as a tertiary protein structure, are provided. A centroid of the residue centroids is calculated. The centroid of the residue centroids is used as a spatial origin of a global linear hydrophobic moment. The correlation between residue centroid magnitude and residue solvent accessibility is enhanced. The global linear hydrophobic moment is defined, wherein each of the residue centroids contributes a magnitude and direction to the global linear hydrophobic moment. A method for comparing at least two tertiary protein structures is also disclosed.

Abstract: Techniques for protein structure analysis are provided. In one aspect, a method of analyzing a multi-domain protein structure comprises the following steps. For at least one domain, a hydrophobic dipole, e.g., defined as a first-order hydrophobic moment of the domain, is calculated. A score representing the orientation of the hydrophobic dipole of the at least one domain relative to a hydrophobic dipole of one or more other domains of the multi-domain protein structure is then calculated.

Abstract: Techniques for protein structure analysis are provided. In one aspect, a method of characterizing at least a portion of a protein structure comprising amino acid residues comprises the following steps. A set of values characterizing the protein structure are determined, wherein each value represents a distance from a center of the protein structure to a center of a given one or more of the amino acid residues. One or more other sets of values characterizing the hydrophobicity of the protein structure are obtained. A Fourier transform is performed on each of the sets of values to obtain transformed values sets. The transformed value sets are compared to correlate the hydrophobicity with the protein structure.

Abstract: A system and method for spatially profiling a distribution of hydrophobicity of a transmembrane protein includes a scaler which generates scaled hydrophobicity values for the transmembrane protein, and a profiler which spatially profiles a hydrophobicity distribution for the transmembrane protein based on the scaled hydrophobicity values.

Abstract: Techniques for analyzing protein structures, such as a tertiary protein structure, are provided. A centroid of the residue centroids is calculated. The centroid of the residue centroids is used as a spatial origin of a global linear hydrophobic moment. The correlation between residue centroid magnitude and residue solvent accessibility is enhanced. The global linear hydrophobic moment is defined, wherein each of the residue centroids contributes a magnitude and direction to the global linear hydrophobic moment. A method for comparing at least two tertiary protein structures is also disclosed.