Protein structure prediction is limited by the inaccuracy of the simplified energy functions necessary for efficient sorting over many conformations. It was recently suggested (Finkelstein, Phys Rev Lett 1998;80:4823-4825) that these errors can be reduced by energy averaging over a set of homologous
Protein folds from pair interactions: A blind test in fold recognition
✍ Scribed by Flöckner, Hannes; Domingues, Francisco S.; Sippl, Manfred J.
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 159 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0887-3585
No coin nor oath required. For personal study only.
✦ Synopsis
We submitted nine predictions to CASP2 using our fold recognition program ProFIT. Two of these structures were still unsolved by the end of the experiment, six had a recognizable fold, and one fold was new. Four predictions of the six recognizable folds were correct. Two models were excellent in terms of alignment quality (T0031, T0004): in one the alignment was partially correct (T0014), and one fold was correctly identified (T0038). We discuss improvements of the program and analyze the prediction results. Proteins, Suppl.
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## Abstract A crucial challenge in present biomedical research is the elucidation of how fundamental processes like protein folding and aggregation occur in the complex environment of the cell. Many new physico‐chemical factors like crowding and confinement must be considered, and immense technical