Predicting the protein-protein interactions using primary structures with predicted protein surface.
BACKGROUND
Many biological functions involve various protein-protein interactions (PPIs). Elucidating such interactions is crucial for understanding general principles of cellular systems. Previous studies have shown the potential of predicting PPIs based on only sequence information. Compared to approaches that require other auxiliary information, these sequence-based approaches can be applied to a broader range of applications.


RESULTS
This study presents a novel sequence-based method based on the assumption that protein-protein interactions are more related to amino acids at the surface than those at the core. The present method considers surface information and maintains the advantage of relying on only sequence data by including an accessible surface area (ASA) predictor recently proposed by the authors. This study also reports the experiments conducted to evaluate a) the performance of PPI prediction achieved by including the predicted surface and b) the quality of the predicted surface in comparison with the surface obtained from structures. The experimental results show that surface information helps to predict interacting protein pairs. Furthermore, the prediction performance achieved by using the surface estimated with the ASA predictor is close to that using the surface obtained from protein structures.


CONCLUSIONS
This work presents a sequence-based method that takes into account surface information for predicting PPIs. The proposed procedure of surface identification improves the prediction performance with an F-measure of 5.1%. The extracted surfaces are also valuable in other biomedical applications that require similar information.
Chang
Darby Tien-Hao
DT
Department of Electrical Engineering, National Cheng Kung University, Tainan, 70101, Taiwan. darby@ee.ncku.edu.tw
Syu
Yu-Tang
YT
Lin
Po-Chang
PC
D000595:Amino Acid Sequence; D001665:Binding Sites; D030562:Databases, Protein; D008958:Models, Molecular; D025941:Protein Interaction Mapping / Q000379:methods*; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D040901:Proteomics / Q000379:methods; D020539:Sequence Analysis, Protein / Q000379:methods; D013329:Structure-Activity Relationship
D011506:Proteins