Interactions between hydrophobic side chains within α‐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...

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Veröffentlicht in:	Protein science 1995-07, Vol.4 (7), p.1305-1314
Hauptverfasser:	Creamer, Trevor P., Rose, George D.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino Acids - chemistry Chemical Phenomena Chemistry, Physical Drug Stability hydrophobicity Models, Chemical Molecular Sequence Data Protein Conformation Protein Folding Protein Structure, Secondary Proteins - chemistry secondary structure Thermodynamics α‐helix
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