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: 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 and uses a set of descriptors of three-dimensional molecular property fields. A portion of the descriptors are calculated in such a way as to separate property fields from the underlying structure of the molecule. These descriptors are calculated through reference to a property field center. Thus, only if the property field changes, such as by moving an atom having a non-zero property value, will the descriptors need to be recalculated. Additionally, a portion of the descriptors do relate to the underlying molecular structure, only these descriptors contain information from more than one reference point. In particular, a displacement is determined between a property field center and the centroid of a molecule. This descriptor contains information from two reference points. Furthermore, components of a property field are mapped onto a principal geometric frame, which essentially references the property field to the molecular shape.

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 and uses a set of descriptors of three-dimensional molecular property fields. A portion of the descriptors are calculated in such as way as to separate property fields from the underlying structure of the molecule. These descriptors are calculated through reference to a property field center. Thus, only if the property field changes, such as by moving an atom having a non-zero property value, will the descriptors need to be recalculated. Additionally, a portion of the descriptors do relate to the underlying molecular structure, only these descriptors contain information from more than one reference point. In particular, a displacement is determined between a property field center and the centroid of a molecule. This descriptor contains information from two reference points. Furthermore, components of a property field are mapped onto a principal geometric frame, which essentially references the property field to the molecular shape.