Prediction of Protein Secondary Structures from Sequences

PREDICTION OF PROTEIN SECONDARY STRUCTURES FROM SEQUENCES 

The enormous structural diversity of proteins begins with different amino acid sequences (primary structure) of polypeptide chains that fold into complex 3D structures. The final folded arrangement of the polypeptide chain is referred to as its conformation (secondary and tertiary structures). It appears that the information for folding to the native conformation is present in the amino acid sequences (Anfinsen, 1973) however, a special class of proteins known as chaperons is required to facilitate in vivo folding of a protein to form its native conformation (Martin and Hartl, 1997). 

Large-scale sequencing projects produce data of genes hence they produce protein sequences at an amazing pace. Although experimental determination of protein three-dimensional structure has become more efficient, the gap between the number of known sequences and the number of known structures is rapidly 

There are four approaches to secondary structure prediction (Fasman, 1989)  

Empirical statistical methods that use parameters derived from known 3D structures (Chou and Fasman, 1974). 

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