HETEROSCEDASTIC DISCRIMINANT ANALYSIS COMBINED WITH FEATURE SELECTION FOR CREDIT SCORING

Credit granting is a fundamental question and one of the most complex tasks that every credit institution is faced with. Typically, credit scoring databases are often large and characterized by redundant and irrelevant features. An effective classification model will objectively help managers instead of intuitive experience. This study proposes an approach for building a credit scoring model based on the combination of heteroscedastic extension (Loog, Duin, 2002) of classical Fisher Linear Discriminant Analysis (Fisher, 1936, Krzyśko, 1990) and a feature selection algorithm that retains sufficient information for classification purpose. We have tested five feature subset selection algorithms: two filters and three wrappers. To evaluate the accuracy of the proposed credit scoring model and to compare it with the existing approaches we have used the German credit data set from the study (Chen, Li, 2010). The results of our study suggest that the proposed hybrid approach is an effective and promising method for building credit scoring models

Model of early stage intermediate in respect to its final structure

The model, describing a method of determining the structure of an early intermediate in the process of protein folding to analyze nonredundant PDB protein bases, allows determining the relationship between the sequence of tetrapeptides and their structural forms expressed by structural codes. The contingency table expressing such a relationship can be used to predict the structure of polypeptides by proposing a structural form with a precision limited to the structural code. However, by analyzing structural forms in native forms of proteins based on the fuzzy oil drop model, one can also determine the status of polypeptide chain fragments with respect to the assumptions of this model. Whether the probability distributions for both compliant and noncompliant forms were similar or whether the tetrapeptide sequences showed some differences at a level of a set of structural codes was investigated. The analysis presented here indicated that some sequences in both forms revealed differences in probability distributions expressed as a negative statistically significant correlation coefficient. This meant that the identified sections (tetrapeptides) took different forms against the fuzzy oil drop model. It may suggest that the information of the final status with respect to hydrophobic core formation is already carried by the structure of the early-stage intermediate

Learning to Unknot

We introduce natural language processing into the study of knot theory, as made natural by the braid word representation of knots. We study the UNKNOT problem of determining whether or not a given knot is the unknot. After describing an algorithm to randomly generate N-crossing braids and their knot closures and discussing the induced prior on the distribution of knots, we apply binary classification to the UNKNOT decision problem. We find that the Reformer and shared-QK Transformer network architectures outperform fully-connected networks, though all perform well. Perhaps surprisingly, we find that accuracy increases with the length of the braid word, and that the networks learn a direct correlation between the confidence of their predictions and the degree of the Jones polynomial. Finally, we utilize reinforcement learning (RL) to find sequences of Markov moves and braid relations that simplify knots and can identify unknots by explicitly giving the sequence of unknotting actions. Trust region policy optimization (TRPO) performs consistently well for a wide range of crossing numbers and thoroughly outperformed other RL algorithms and random walkers. Studying these actions, we find that braid relations are more useful in simplifying to the unknot than one of the Markov moves

Pion and Kaon Distribution Amplitudes from lattice QCD: towards the continuum limit

We present the current status of a non-perturbative lattice calculation of the moments of the pion and kaon distribution amplitudes by the RQCD collaboration. Our investigation is carried out using $N_f=2+1$ dynamical, non-perturbatively O(a)-improved Wilson fermions on the CLS ensembles with 5 different lattice spacings and pion masses down to the physical pion mass. A combined continuum and chiral extrapolation to the physical point is performed along two independent quark mass trajectories simultaneously. We employ momentum smearing in order to decrease the contamination by excited states and increase statistical precision.Comment: Proceedings of the 36th Annual International Symposium on Lattice Field Theory - LATTICE201

The Two Faces of the Liquid Ordered Phase

Coexisting liquid ordered (L-o) and liquid disordered (L-d) lipid phases in synthetic and plasma membrane-derived vesicles are commonly used to model the heterogeneity of biological membranes, including their putative ordered rafts. However, raft-associated proteins exclusively partition to the L-d and not the L-o phase in these model systems. We believe that the difference stems from the different microscopic structures of the lipid rafts at physiological temperature and the L-o phase studied at room temperature. To probe this structural diversity across temperatures, we performed atomistic molecular dynamics simulations, differential scanning calorimetry, and fluorescence spectroscopy on L-o phase membranes. Our results suggest that raftassociated proteins are excluded from the L-o phase at room temperature due to the presence of a stiff, hexagonally packed lipid structure. This structure melts upon heating, which could lead to the preferential solvation of proteins by order-preferring lipids. This structural transition is manifested as a subtle crossover in membrane properties; yet, both temperature regimes still fulfill the definition of the L-o phase. We postulate that in the compositionally complex plasma membrane and in vesicles derived therefrom, both molecular structures can be present depending on the local lipid composition. These structural differences must be taken into account when using synthetic or plasma membrane-derived vesicles as a model for cellular membrane heterogeneity below the physiological temperature.Peer reviewe

Divergence entropy-based evaluation of hydrophobic core in aggressive and resistant forms of transthyretin

The two forms of transthyretin differing slightly in the tertiary structure, despite the presence of five mutations, show radically different properties in terms of susceptibility to the amyloid transformation process. These two forms of transthyretin are the object of analysis. The search for the sources of these differences was carried out by means of a comparative analysis of the structure of these molecules in their native and early intermediate stage forms in the folding process. The criterion for assessing the degree of similarity and differences is the status of the hydrophobic core. The comparison of the level of arrangement of the hydrophobic core and its initial stages is possible thanks to the application of divergence entropy for the early intermediate stage and for the final forms. It was shown that the minimal differences observed in the structure of the hydrophobic core of the forms available in PDB, turned out to be significantly different in the early stage (ES) structure in folding process. The determined values of divergence entropy for both ES forms indicate the presence of the seed of hydrophobic core only in the form resistant to amyloid transformation. In the form of aggressively undergoing amyloid transformation, the structure lacking such a seed is revealed, being a stretched one with a high content of β-type structure. In the discussed case, the active presence of water in the structural transformation of proteins expressed in the fuzzy oil drop model (FOD) is of decisive importance for the generation of the final protein structure. It has been shown that the resistant form tends to generate a centric hydrophobic core with the possibility of creating a globular structure, i.e., a spherical micelle-like form. The aggressively transforming form reveals in the structure of its early intermediate, a tendency to form the ribbon-like micelle as observed in amyloid

Structure of the hydrophobic core determines the 3D protein structure-verification by single mutation proteins

Four de novo proteins differing in single mutation positions, with a chain length of 56 amino acids, represent diverse 3D structures: monomeric 3$\alpha$ and 4$\beta$ + $\alpha$ folds. The reason for this diversity is seen in the different structure of the hydrophobic core as a result of synergy leading to the generation of a system in which the polypeptide chain as a whole participates. On the basis of the fuzzy oil drop model, where the structure of the hydrophobic core is expressed by means of the hydrophobic distribution function in the form of a 3D Gaussian distribution, it has been shown that the composition of the hydrophobic core in these two structural forms is different. In addition, the use of a model to determine the structure of the early intermediate in the folding process allows to indicate differences in the polypeptide chain geometry, which, combined with the construction of a common hydrophobic nucleus as an effect of specific synergy, may indicate the reason for the diversity of the folding process of the polypeptide chain. The results indicate the need to take into account the presence of an external force field originating from the water environment and that its active impact on the formation of a hydrophobic core whose participation in the stabilization of the tertiary structure is fundamental

Gallbladder cancer- causes, symptoms and chirurgical treatment: systematic review

Gallbladder cancer (GBC) is the most common cancer of bile ducts. This is one of the worst prognostic tumors of the digestive tract. The disease is asymptomatic for a long time, which is why it is detected in a high stage, which shortens the chances of healing. Surgery has a fundamental role in the treatment of gallbladder cancer. The patient survival prognosis depends mainly on the local severity of the disease, distant metastases and the radicality of surgical resection (R0)

Light-cone distribution amplitudes of octet baryons from lattice QCD

We present lattice QCD results for the wave function normalization constants and the first moments of the distribution amplitudes for the lowest-lying baryon octet. The analysis is based on a large number of $N_f=2+1$ ensembles comprising multiple trajectories in the quark mass plane including physical pion (and kaon) masses, large volumes, and, most importantly, five different lattice spacings down to $a=0.039\,\mathrm{fm}$. This allows us to perform a controlled extrapolation to the continuum and infinite volume limits by a simultaneous fit to all available data. We demonstrate that the formerly observed violation of flavor symmetry breaking constraints can, indeed, be attributed to discretization effects that vanish in the continuum limit

The structure of amyloid versus the structure of globular proteins

The issue of changing the structure of globular proteins into an amyloid form is in the focus of researchers' attention. Numerous experimental studies are carried out, and mathematical models to define the essence of amyloid transformation are sought. The present work focuses on the issue of the hydrophobic core structure in amyloids. The form of ordering the hydrophobic core in globular proteins is described by a 3D Gaussian distribution analog to the distribution of hydrophobicity in a spherical micelle. Amyloid fibril is a ribbon-like micelle made up of numerous individual chains, each representing a flat structure. The distribution of hydrophobicity within a single chain included in the fibril describes the 2D Gaussian distribution. Such a description expresses the location of polar residues on a circle with a center with a high level of hydrophobicity. The presence of this type of order in the amyloid forms available in Preotin Data Bank (PDB) (both in proto- and superfibrils) is demonstrated in the present work. In this system, it can be assumed that the amyloid transformation is a chain transition from 3D Gauss ordering to 2D Gauss ordering. This means changing the globular structure to a ribbon-like structure. This observation can provide a simple mathematical model for simulating the amyloid transformation of proteins