A comprehensive analysis of 40 blind protein structure predictions.

ABSTRACT:

Background

We thoroughly analyse the results of 40 blind predictions for which an experimental answer was made available at the fourth meeting on the critical assessment of protein structure methods (CASP4). Using our comparative modelling and fold recognition methodologies, we made 29 predictions for targets that had sequence identities ranging from 50% to 10% to the nearest related protein with known structure. Using our ab initio methodologies, we made eleven predictions for targets that had no detectable sequence relationships.

Results

For 23 of these proteins, we produced models ranging from 1.0 to 6.0 A root mean square deviation (RMSD) for the Calpha atoms between the model and the corresponding experimental structure for all or large parts of the protein, with model

SUBMITTER: Samudrala R 

PROVIDER: S-EPMC122083 | biostudies-literature | 2002 Aug

REPOSITORIES: biostudies-literature