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Noncharged amino acid residues at the solvent-exposed positions in the middle and at the C terminus of the α-helix have the same helical propensity

It was established previously that helical propensities of different amino acid residues in the middle of α-helix in peptides and in proteins are very similar. The statistical analysis of the protein helices from the known three-dimensional structures shows no difference in the frequency of noncharg...

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Main Authors: Ermolenko, Dmitri N., Richardson, John M., Makhatadze, George I.
Formato: Artigo
Idioma:Inglês
Publicado: Cold Spring Harbor Laboratory Press 2003
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Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC2323897/
https://ncbi.nlm.nih.gov/pubmed/12761387
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