That is because structure determines function of the protein. Take the example of enzyme dehydrogenases. It has an NAD-binding site called Rossaman fold ( Dinucleotide binding fold). This fold is made up a pair of βαβαβ subunit. Thus if a protein contain a βαβαβ subunit than it acts as a binding site for a nucleotide.
Structure is better conserved than sequences in protein during the course of evolution e.g. take the example of Cytochrome C of eukaryotes and C-cytochromes of prokaryotes in different species(which change with evolution in prokaryotes) where all perform general functions i.e. electron carrier. But different species exibit low degree of similarity of sequence to each other and to that of eukaryotes. They also differ in polypeptide loops on surface. But X-Ray structure are similar particularly chain folds and side chain packing to interior.
We require structural knowledge for rational drug design, protein engineering, for detail study of protein-biomolecule interactions.
Experimental methods to find structure of protein
Other methods are Cryo-EM(electron microscopy),
X-Ray Crystallography, NMR, Cryo-EM gives 3D information of proteins but CD only gives one dimensional structure of protein i.e. secondary structure only
Why do we want predicted methods ??
Computer based prediction are much easier to handle with. E.g. one is free to make errors with out compensating much as it is inexpensive at least in future. Moreover we don't have always sufficient material for experimental methods. Some proteins even don't crystallize. So we turn to predicted method if experimental methods fail.
Computation Method of structure prediction
- Secondary structure prediction
- Protein Threading or Fold Family Recognition
- Ab-initio structure prediction
- Homology Modeling