Bioinformatics Vol. 18 no. 5 2002
Pages 697-704
© 2002 Oxford University Press
Characterization of the folding degree of proteins
Faculty of Pharmacy, Department of Organic Chemistry, University of Santiago de Compostela, 15706 Santiago de Compostela, Spain
Received on August 20, 2001
; revised on October 20, 2001
; accepted on November 23, 2001
Motivation: The characterization of the folding degree of chains is central to the elucidation of structure--function relationships in proteins. Here we present a new index for characterizing the folding degree of a (protein) chain. This index shows a range of features that are desirable for the study of the relation between structure and function in proteins.
Results: A novel index characterizing the folding degree of
(protein) chains is developed based on the spectral moments of a matrix
representing the dihedral angles (
, 
and 
) of the protein
main chain. The proposed index is normalized to the chain size, is not
correlated to the gyration radius of the backbone chain and is able to
distinguish between structures for which the sum of the main-chain dihedral
angles is identical. The index is well correlated to the percentages of
helix and strand in proteins, shows a linear dependence with temperature
changes, and is able to differentiate among protein families.
Availability: On request from the author.
Contact: estrada66{at}yahoo.com