| Popis: |
Traditional approaches to sequence alignment are based on evolutionary ideas. As a result, they are prebiased toward results which are in accord with initial expectations. We present here a method of sequence alignment which is based entirely on the physical properties of the amino acids. This approach has no inherent bias, eliminates much of the computational complexity associated with methods currently in use, and has been shown to give good results for structures which were poorly predicted by traditional methods in recent CASP competitions and to identify sequence differences which correlate with structural and dynamic differences not detectable by traditional methods. |
