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Interactions between hydrophobic side chains within alpha-helices.

The thermodynamic basis of helix stability in peptides and proteins is a topic of considerable interest. Accordingly, we have computed the interactions between side chains of all hydrophobic residue pairs and selected triples in a model helix, using Boltzmann-weighted exhaustive modeling. Specifical...

詳細記述

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書誌詳細
主要な著者: Creamer, T. P., Rose, G. D.
フォーマット: Artigo
言語:Inglês
出版事項: Cold Spring Harbor Laboratory Press 1995
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC2143171/
https://ncbi.nlm.nih.gov/pubmed/7670373
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