The use of folding patterns in the prediction of protein topologies.
We proved previously that the distribution of formation energies which may be associated with the predicted secondary structures (or nuclei) is specific of the folding process (Busetta, B. 1986, Biochim. Biophys. Acta 870, 327-338). We developed a new predictive algorithm for protein topologies, based on the search of standard 'folding patterns'. In another manner, the strongest predicted nuclei are used to propose a fast sequence-alignment process which is efficient for distantly related proteins.
Busetta
B
B
Laboratoire de Cristallographie U.A. 144 C.N.R.S., Talence, France.
D000426:Alcohol Dehydrogenase; D000465:Algorithms; D000595:Amino Acid Sequence; D000818:Animals; D004284:Dogfish; D006736:Horses; D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase; D011487:Protein Conformation; D011506:Proteins / Q000145:classification*
D007527:Isoenzymes; D011506:Proteins; D000426:Alcohol Dehydrogenase; D007770:L-Lactate Dehydrogenase