A beta/gamma motif to mimic alpha-helical turns in proteins

Autor:	Araghi, Raheleh Rezaei, Jäckel, Christian, Salwiczek, Mario, Wagner, Sara C., Wieczorek, Sebastian, Baldauf, Carsten, Koksch, Beate, Cölfen, Helmut, Völkel, Antje
Rok vydání:	2009
Předmět:	alpha-helical coiled coil peptidomimetics Circular Dichroism ddc:540 Amino Acid Motifs beta/gamma-peptides Proteins foldamers Amino Acid Sequence Amino Acids Molecular Dynamics Simulation protein design Protein Structure Secondary
Zdroj:	Chembiochem : a European journal of chemical biology. 11(3)
ISSN:	1439-7633
Popis:	The combination of the properties of β- and γ-amino acids produce extended artificial fragments that recreate the properties of a natural α-helix. The substitution of two α-helical turns in an otherwise natural coiled-coil motif by a fragment of alternating β and γ-amino acids with retention of global conformation and stability of the fold was established. The new chimeric system shows a high potency in helical quaternary structure formation.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::0f8bdfbf967cce79fdf693bc0cde7b68 https://pubmed.ncbi.nlm.nih.gov/20039254 Zobrazit plný text záznamu Plný text