arXiv · physics/0211033
Distances and classification of amino acids for different protein secondary structures
Abstract
Window profiles of amino acids in protein sequences are taken as a description of the amino acid environment. The relative entropy or Kullback-Leibler distance derived from profiles is used as a measure of dissimilarity for comparison of amino acids and secondary structure conformations. Distance matrices of amino acid pairs at different conformations are obtained, which display a non-negligible dependence of amino acid similarity on conformations. Based on the conformation specific distances clustering analysis for amino acids is conducted.
Explore related subjects
Keep this discovery
Xin Liu, Li-mei Zhang, Shan Guan, Wei-Mou Zheng. 2003-06-16. Distances and classification of amino acids for different protein secondary structures. https://doi.org/10.1103/physreve.67.051927
Cite the original work for its findings. Save a collection to share your selection of sources.