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Analysis of accessible surface of residues in proteins

We analyzed the total, hydrophobic, and hydrophilic accessible surfaces (ASAs) of residues from a nonredundant bank of 587 3D structure proteins. In an extended fold, residues are classified into three families with respect to their hydrophobicity balance. As expected, residues lose part of their so...

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Detalhes bibliográficos
Main Authors: Lins, Laurence, Thomas, Annick, Brasseur, Robert
Formato: Artigo
Idioma:Inglês
Publicado em: Wiley-Blackwell 2003
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Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2323943/
https://ncbi.nlm.nih.gov/pubmed/12824487
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