A new Technique in Protein Structure Quantitative Identification

Abstract

Graph distance is also named approximate graph isomorphism, error-tolerant graph matching, it is a measure of similarity (or dissimilarity) between two graphs. The graph distance function is an elusive question remaining a pressing problem in a wide range of fields. In general, graphs are usually enriched with node and edge attributes, namely, heterogeneous graphs, our focus is encapsulating node and edge identities in a graph. In addition, an adequate representation of the graph-adjacency matrix can capture the connectivity of the graph structure, while an adjacency matrix bears high-order combinatorial nature. Solving these challenges in the effective analysis of these graphs is of utmost importance. In this paper, structural and semantic features are both preserved by graphs, so the analysis of row sum and eigenspectra for vertex and edge adjacency matrix has captured the affinity interactions within graphs locally and globally. Therefore, we estimate the geometrical and semantic dissimilarities/distances between graphs extensively and systemically. Several illustrative chemical compound cases implement in practical scenarios, thus, the theory could be easily understood. Our method defines a quantitative distance (or dissimilarity) measure for comparing graphs, it has a good measure of expressiveness and a suited polynomial computation complexity, which paves the way for graph analysis.