We hypothesize that proteins of the same homology contain conserved hydrophobic residues and exhibit analogous residue interaction patterns in the folded state.
We hypothesize that proteins of the same homology contain conserved hydrophobic residues and exhibit analogous residue interaction patterns in the folded state.
Aug 1, 2008 · In this work, we propose a graph-theory-based data mining framework to extract and isolate protein structural features that sustain invariance ...
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In this work, we propose a graph-theory-based data mining framework to extract and isolate protein structural features that sustain invariance in evolutionary- ...
Oct 20, 2015 · In this work, we propose a graph-theory-based data mining framework to extract and isolate protein structural features that sustain invariance ...
In this work, we propose a graph-theory-based data mining framework to extract and isolate protein structural features that sustain invariance in evolutionary- ...
Abstract. Evolutionarily conserved hydrophobic residues at the core of protein structures are generally assumed to play a structural role in protein foldin.
We hypothesize that proteins of the same homology contain conserved hydrophobic residues and exhibit analogous residue interaction patterns in the folded state.
Pradeep Chowriappa, Sumeet Dua, Jinko Kanno and Hilary W. Thompson. "Protein Structure Classification Based on Conserved Hydrophobic Residues" IEEE/ACM ...
Here, we investigate the extent to which these conserved residues are clustered in three-dimensional protein structures. In 92% of the proteins in a data set of ...
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