A statistical analytical approach has been used to analyze the secondary structure (SS) of amino acids as a function of the
sequence of amino acid residues. We have used 306 non-homologous best-resolved protein structures from the Protein Data Bank
for the analysis. A sequence region of 32 amino acids on either side of the residue is considered in order to calculate single
amino acid propensities, di-amino acid potentials and tri-amino acid potentials. A weighted sum of predictions obtained using
these properties is used to suggest a final prediction method. Our method is as good as the best-known SS prediction methods,
is the simplest of all the methods, and uses no homologous sequence/family alignment data, yet gives 72% SS prediction accuracy.
Since the method did not use many other factors that may increase the prediction accuracy there is scope to achieve greater
accuracy using this approach.
Received: 4 May 1998 / Accepted: 17 September 1998 / Published online: 10 December 1998 相似文献
A new method to control the morphology and functionality of micelles is reported. Triblock copolymer micelles with atom transfer radical polymerization initiators at the interface are prepared in aqueous solution. After in‐situ polymerization at the interface, the structures of the interface and corona change, and micelles with PDMAEMA‐PEG comb–coil coronal chains are obtained. In aqueous solution, the pH exerts an influence on the morphology of the micelles. The coronal chains adopt different conformations at different pH values. Upon drying, the two coronal chains phase separate and form nanometer‐sized domains.
