Folding of beta pep-4 beta-sheet sandwich dimers and tetramers is influenced by aliphatic hydrophobic residues at the intersubunit interface.

For the designed peptide 33mer, beta pep-4, formation of beta-sheet structure [Ilyina, Roongta and Mayo (1997) Biochemistry 36, 5245--5250] is thermodynamically linked to self-association. Dimers and tetramers are stabilized by interactions between hydrophobic residues lying on the hydrophobic faces...

Ausführliche Beschreibung

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Bibliographische Detailangaben
Hauptverfasser: Cox, A, Arroyo, M M, Mayo, K H
Format: Artigo
Sprache:Inglês
Veröffentlicht: 2001
Schlagworte:
Research Article
Online Zugang:https://ncbi.nlm.nih.gov/pmc/articles/PMC1222003/
https://ncbi.nlm.nih.gov/pubmed/11463344
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