Identifying Similar Patterns of Structural Flexibility in Proteins by Disorder Prediction and Dynamic Programming

International Journal of Molecular Sciences

Adam Borne¹  Bin Xue¹  Vladimir N. Uversky²  Aidan Petrovich³ 

[1] Department of Cell Biology, Microbiology, and Molecular Biology,School of Natural Sciences and Mathematics, College of Arts and Sciences,University of South Florida, Tampa, FL 33620, USA;Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute,Morsani College of Medicine, University of South Florida, Tampa, FL 33620, USA;Department of Physics, University of South Florida, Tampa, FL 33620, USA;

关键词: intrinsic disorder;    structural flexibility;    disorder pattern;    dynamic programming;    dynamic time warping;   

DOI  :  10.3390/ijms160613829

来源: DOAJ

【 摘 要 】

Computational methods are prevailing in identifying protein intrinsic disorder. The results from predictors are often given as per-residue disorder scores. The scores describe the disorder propensity of amino acids of a protein and can be further represented as a disorder curve. Many proteins share similar patterns in their disorder curves. The similar patterns are often associated with similar functions and evolutionary origins. Therefore, finding andcharacterizing specific patterns of disorder curves provides a unique and attractive perspective of studying the function of intrinsically disordered proteins. In this study, we developeda new computational tool named IDalign using dynamic programming. This tool is ableto identify similar patterns among disorder curves, as well as to present the distribution of intrinsic disorder in query proteins. The disorder-based information generated by IDalign is significantly different from the information retrieved from classical sequence alignments. This tool can also be used to infer functions of disordered regions and disordered proteins. The web server of IDalign is available at (http://labs.cas.usf.edu/bioinfo/service.html).

【 授权许可】

Unknown