Conservation and prediction of solvent accessibility in protein families

@article{Rost1994ConservationAP,
  title={Conservation and prediction of solvent accessibility in protein families},
  author={Burkhard Rost and Chris Sander},
  journal={Proteins: Structure},
  year={1994},
  volume={20}
}
Currently, the prediction of three‐dimensional (3D) protein structure from sequence alone is an exceedingly difficult task. As an intermediate step, a much simpler task has been pursued extensively: predicting 1D strings of secondary structure. Here, we present an analysis of another 1D projection from 3D structure: the relative solvent accessibility of each residue. We show that solvent accessibility is less conserved in 3D homologues than is secondary structure, and hence is predicted less… 
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TLDR
A new threading method for detecting remote 3D homologues of PDB proteins by projecting 3D structure onto 1D strings of secondary structure and relative solvent accessibility and aligned by dynamic programming.
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A suite of five methods for prediction of solvent accessibility prediction over a large dataset and a metamethod based on an ensemble average of the individual methods, leading to a two-state classification accuracy of 80% are refined and suggested to be a valuable tool in improving protein structure prediction.
PROFcon: novel prediction of long-range contacts
TLDR
PROFcon, a novel contact prediction method that combines information from alignments, from predictions of secondary structure and solvent accessibility, from the region between two residues and from the average properties of the entire protein, is introduced.
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