ISSN:
0887-3585
Keywords:
protein structure prediction
;
potentials of mean force
;
ab initio folding
;
structural motifs
;
simulated annealing
;
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Medicine
Notes:
A simple approach to protein tertiary structure prediction is described, based on the assembly of recognized supersecondary structural fragments taken from highly resolved protein structures by using a simulated annealing algorithm. The results of blind-testing this method on CASP2 target T0042 (pig NK-lysin) are presented. The predicted structure had a Cα root-mean-square deviation of only 6.2 Å from the experimental structure (and less than 5.0 Å over the first 66 residues), and clearly had the correct fold when judged by using a number of objective measures. Despite the significant degree of success in this case, there is clearly much more development required before predictions with the accuracy of a good homology model can be made with this kind of approach. Proteins, Suppl. 1:185-191, 1997. © 1998 Wiley-Liss, Inc.
Additional Material:
3 Ill.
Type of Medium:
Electronic Resource
