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| Title: | Bridging the protein sequence-structure gap by predictions? |
| Author: | Burkhard Rost & Chris Sander |
| Quote: | Annual Review of Biophysics and Biomolecular Structure , 25, 113-136 (1996) |
The problem of accurately predicting protein three-dimensional structure from sequence has yet to be solved. Recently, a number of new and promising methods that work in one, two or three dimensions have invigorated the field. Modelling by homology can yield fairly accurate three-dimensional structures for about 25% of the currently known protein sequences. Techniques for cooperatively fitting sequences into known three-dimensional folds, called threading methods, are capable of increasing this rate by detecting very remote homologies in favourable cases. Prediction of protein structure in two dimension, i.e., prediction of inter-residue contacts, is in its infancy. Prediction tools that work in one dimension are both mature and generally applicable; they predict secondary structure, residue solvent accessibility, and the location of transmembrane helices with reasonable accuracy. These and other prediction methods have gained immensely from the rapid increase of information in publicly accessible databases. Growing databases will lead to further improvements of prediction methods and thus to narrowing the gap between the number of known protein sequences and known protein structures.