The evolution of protein structures. The predicted structure of immunoglobulin D1.3 and its comparison with the crystal structure. Conformations of immunoglobulin hypervariable regions. Failures of inverse folding and threading with gapped alignment. Assigning amino acid sequences to 3-dimensional protein folds.
Protein fold recognition.
Successful protein fold recognition by optimal sequence threading validated by rigorous blind testing. A Practical Approach . Assessment of protein models with three-dimensional profiles. CATH- A Hierarchic Classification of Protein Domain Structures. A 3D-1D substitution matrix for protein fold recognition that includes predicted secondary structure of the sequence.