Hydrophobic tint of knot proteins

Protein structures having knotted configurations in their native fold, have great impact in their function. Protein knot localization has become possible in single molecule experiments though they are identified in their structure level. Signal processing methods which have played an important role to analyse genomic and proteomic sequences are also useful for knot protein analysis. The amino acid index hydrophobicity contributes the knowledge of stability of proteins. Water capture and release is found to be controllable by the tightening force in knots which are related to this index. It is observed that, the knot proteins are of hydrophobic in nature by Fourier analysis, Power spectral density estimation and Cross correlation method. The set of knot proteins from proteinKNOT web server(pKNOT) has been used for the experimentation and proved 93% of them are of hydrophobic nature in their knotted core.