Correlated mutations and residue contacts in proteins

@article{Gbel1994CorrelatedMA,
  title={Correlated mutations and residue contacts in proteins},
  author={Ulrike G{\"o}bel and Chris Sander and Reinhard Schneider and Alfonso Valencia},
  journal={Proteins: Structure},
  year={1994},
  volume={18}
}
The maintenance of protein function and structure constrains the evolution of amino acid sequences. This fact can be exploited to interpret correlated mutations observed in a sequence family as an indication of probable physical contact in three dimensions. Here we present a simple and general method to analyze correlations in mutational behavior between different positions in a multiple sequence alignment. We then use these correlations to predict contact maps for each of 11 protein families… 

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Improvements in structural contact prediction: opportunities in prediction diculty and pairing preference of amino acids

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    Advances in experimental medicine and biology
  • 2018
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An introduction to protein contact prediction.

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Direct coupling analysis for protein contact prediction.

Direct Coupling Analysis has been shown to produce highly accurate estimates of amino-acid pairs that have direct reciprocal constraints in evolution and instructions and protocols on how to use the algorithmic implementations of DCA starting from data extraction to predicted-contact visualization in contact maps or representative protein structures are provided.

Coevolutionary Signals and Structure-Based Models for the Prediction of Protein Native Conformations.

This chapter introduces a general and efficient methodology to perform coevolutionary analysis on protein sequences and to use this information in combination with computational physical models to predict the native 3D conformation of functional polypeptides.
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