Simple solvation potential for coarse-grained models of proteins

We formulate a simple solvation potential based on a coarsed-grain representation of amino acids with two spheres modeling the $C_\alpha$ atom and an effective side-chain centroid. The potential relies on a new method for estimating the buried area of residues, based on counting the effective number of burying neighbours in a suitable way. This latter quantity shows a good correlation with the buried area of residues computed from all atom crystallographic structures. We check the discriminatory power of the solvation potential alone to identify the native fold of a protein from a set of decoys and show the potential to be considerably selective.Comment: 18 pages, 8 tables, 3 figure

Efficient, sparse representation of manifold distance matrices for classical scaling

Geodesic distance matrices can reveal shape properties that are largely invariant to non-rigid deformations, and thus are often used to analyze and represent 3-D shapes. However, these matrices grow quadratically with the number of points. Thus for large point sets it is common to use a low-rank approximation to the distance matrix, which fits in memory and can be efficiently analyzed using methods such as multidimensional scaling (MDS). In this paper we present a novel sparse method for efficiently representing geodesic distance matrices using biharmonic interpolation. This method exploits knowledge of the data manifold to learn a sparse interpolation operator that approximates distances using a subset of points. We show that our method is 2x faster and uses 20x less memory than current leading methods for solving MDS on large point sets, with similar quality. This enables analyses of large point sets that were previously infeasible.Comment: Conference CVPR 201

Empirical Potential Function for Simplified Protein Models: Combining Contact and Local Sequence-Structure Descriptors

An effective potential function is critical for protein structure prediction and folding simulation. Simplified protein models such as those requiring only $C_\alpha$ or backbone atoms are attractive because they enable efficient search of the conformational space. We show residue specific reduced discrete state models can represent the backbone conformations of proteins with small RMSD values. However, no potential functions exist that are designed for such simplified protein models. In this study, we develop optimal potential functions by combining contact interaction descriptors and local sequence-structure descriptors. The form of the potential function is a weighted linear sum of all descriptors, and the optimal weight coefficients are obtained through optimization using both native and decoy structures. The performance of the potential function in test of discriminating native protein structures from decoys is evaluated using several benchmark decoy sets. Our potential function requiring only backbone atoms or $C_\alpha$ atoms have comparable or better performance than several residue-based potential functions that require additional coordinates of side chain centers or coordinates of all side chain atoms. By reducing the residue alphabets down to size 5 for local structure-sequence relationship, the performance of the potential function can be further improved. Our results also suggest that local sequence-structure correlation may play important role in reducing the entropic cost of protein folding.Comment: 20 pages, 5 figures, 4 tables. In press, Protein

Online context recognition in multisensor systems using Dynamic Time Warping

In this paper, we present our system for online context recognition of multimodal sequences acquired from multiple sensors. The system uses Dynamic Time Warping (DTW) to recognize multimodal sequences of different lengths, embedded in continuous data streams. We evaluate the performance of our system on two real world datasets: 1) accelerometer data acquired from performing two hand gestures and 2) NOKIA\u27s benchmark dataset for context recognition. The results from both datasets demonstrate that the system can perform online context recognition efficiently and achieve high recognition accuracy.<br /

Potential function of simplified protein models for discriminating native proteins from decoys: Combining contact interaction and local sequence-dependent geometry

An effective potential function is critical for protein structure prediction and folding simulation. For simplified models of proteins where coordinates of only $C_\alpha$ atoms need to be specified, an accurate potential function is important. Such a simplified model is essential for efficient search of conformational space. In this work, we present a formulation of potential function for simplified representations of protein structures. It is based on the combination of descriptors derived from residue-residue contact and sequence-dependent local geometry. The optimal weight coefficients for contact and local geometry is obtained through optimization by maximizing margins among native and decoy structures. The latter are generated by chain growth and by gapless threading. The performance of the potential function in blind test of discriminating native protein structures from decoys is evaluated using several benchmark decoy sets. This potential function have comparable or better performance than several residue-based potential functions that require in addition coordinates of side chain centers or coordinates of all side chain atoms.Comment: 4 pages, 2 figures, Accepted by 26th IEEE-EMBS Conference, San Francisc