Review of nonlinear analysis of proteins through recurrence quantification.
This review considers the use of a nonlinear signal analysis tool, recurrence quantification analysis, as a method to study sequence/structure relationships of proteins. Four broad categories are discussed: (1) a point of view involving information contained in deterministic aspects of hydrophobicity; (2) the analysis of protein hydrophobicity "singularities"; (3) time-series analysis of protein dynamics simulations; and (4) prediction of protein secondary structure.
Zbilut
Joseph P
JP
Department of Molecular Biophysics and Physiology, Rush University, Chicago, IL 60612, USA. Joseph_P_Zbilut@rush.edu
Sirabella
Paolo
P
Giuliani
Alessandro
A
Manetti
Cesare
C
Colosimo
Alfredo
A
Webber
Charles L
CL
D000465:Algorithms; D008962:Models, Theoretical; D009154:Mutation; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000032:analysis* / Q000737:chemistry*; D013997:Time Factors; D014867:Water / Q000737:chemistry; D001618:beta-Lactamases / Q000737:chemistry
D011506:Proteins; D014867:Water; D001618:beta-Lactamases