Computing and graphing probability values of pearson distributions: a SAS/IML macro

Background Any empirical data can be approximated to one of Pearson distributions using the first four moments of the data (Elderton WP, Johnson NL. Systems of Frequency Curves. 1969; Pearson K. Philos Trans R Soc Lond Ser A. 186:343–414 1895; Solomon H, Stephens MA. J Am Stat Assoc. 73(361):153–60 1978). Thus, Pearson distributions made statistical analysis possible for data with unknown distributions. There are both extant, old-fashioned in-print tables (Pearson ES, Hartley HO. Biometrika Tables for Statisticians, vol. II. 1972) and contemporary computer programs (Amos DE, Daniel SL. Tables of percentage points of standardized pearson distributions. 1971; Bouver H, Bargmann RE. Tables of the standardized percentage points of the pearson system of curves in terms of β1 and β2. 1974; Bowman KO, Shenton LR. Biometrika. 66(1):147–51 1979; Davis CS, Stephens MA. Appl Stat. 32(3):322–7 1983; Pan W. J Stat Softw. 31(Code Snippet 2):1–6 2009) available for obtaining percentage points of Pearson distributions corresponding to certain pre-specified percentages (or probability values; e.g., 1.0%, 2.5%, 5.0%, etc.), but they are little useful in statistical analysis because we have to rely on unwieldy second difference interpolation to calculate a probability value of a Pearson distribution corresponding to a given percentage point, such as an observed test statistic in hypothesis testing. Results The present study develops a macro program to identify the appropriate type of Pearson distribution based on either input of dataset or the values of four moments and then compute and graph probability values of Pearson distributions for any given percentage points. Conclusions The SAS macro program returns accurate approximations to Pearson distributions and can efficiently facilitate researchers to conduct statistical analysis on data with unknown distributions.

iPBAvizu: a PyMOL plugin for an efficient 3D protein structure superimposition approach

Background Protein 3D structure is the support of its function. Comparison of 3D protein structures provides insight on their evolution and their functional specificities and can be done efficiently via protein structure superimposition analysis. Multiple approaches have been developed to perform such task and are often based on structural superimposition deduced from sequence alignment, which does not take into account structural features. Our methodology is based on the use of a Structural Alphabet (SA), i.e. a library of 3D local protein prototypes able to approximate protein backbone. The interest of a SA is to translate into 1D sequences into the 3D structures. Results We used Protein blocks (PB), a widely used SA consisting of 16 prototypes, each representing a conformation of the pentapeptide skeleton defined in terms of dihedral angles. Proteins are described using PB from which we have previously developed a sequence alignment procedure based on dynamic programming with a dedicated PB Substitution Matrix. We improved the procedure with a specific two-step search: (i) very similar regions are selected using very high weights and aligned, and (ii) the alignment is completed (if possible) with less stringent parameters. Our approach, iPBA, has shown to perform better than other available tools in benchmark tests. To facilitate the usage of iPBA, we designed and implemented iPBAvizu, a plugin for PyMOL that allows users to run iPBA in an easy way and analyse protein superimpositions. Conclusions iPBAvizu is an implementation of iPBA within the well-known and widely used PyMOL software. iPBAvizu enables to generate iPBA alignments, create and interactively explore structural superimposition, and assess the quality of the protein alignments.