We present our predictions in the ab initio structure prediction category of CASP3. Eleven targets were folded, using a method based on a Monte Carlo search driven by secondary and tertiary restraints derived from multiple sequence alignments. Our results can be qualitatively summarized as follows:
Evolutionary information for specifying a protein fold
β Scribed by Socolich, Michael; Lockless, Steve W.; Russ, William P.; Lee, Heather; Gardner, Kevin H.; Ranganathan, Rama
- Book ID
- 109894687
- Publisher
- Nature Publishing Group
- Year
- 2005
- Tongue
- English
- Weight
- 544 KB
- Volume
- 437
- Category
- Article
- ISSN
- 0028-0836
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Short segments of polypeptide, from a protein for which the primary sequence but not the three-dimensional structure is known, are compared to a library of known structures. The basis of comparison is the probability with which residues in the unknown segment might substitute through evolution for r
## Abstract The search for efficient and predictive methods to describe the protein folding process at the allβatom level remains an important grandβcomputational challenge. The development of multiβteraflop architectures, such as the IBM BlueGene used in this study, has been motivated in part by t