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Back Cover: Induced Folding of Protein‐Sized Foldameric β‐Sandwich Models with Core β‐Amino Acid Residues (Chem. Eur. J. 16/2015)
Author(s) -
Olajos Gábor,
Hetényi Anasztázia,
Wéber Edit,
Németh Lukács J.,
Szakonyi Zsolt,
Fülöp Ferenc,
Martinek Tamás A.
Publication year - 2015
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201590066
Subject(s) - amino acid , residue (chemistry) , chemistry , amino acid residue , folding (dsp implementation) , protein design , protein folding , protein engineering , common core , core (optical fiber) , cover (algebra) , protein secondary structure , protein structure , combinatorial chemistry , biochemistry , peptide sequence , materials science , structural engineering , engineering , enzyme , mechanical engineering , gene , composite material
The β‐sandwich structure is the target of many de novo engineered protein mimetics. In the foldameric approach, α‐amino acids are replaced by unnatural building blocks, which have major effects on the secondary structure in a residue‐dependent way. In their Full Paper on page 6173 ff. , T. Martinek and co‐workers carried out β‐amino acid mutations in the hydrophobic core of a β‐sandwich template by using a diverse set of building blocks. It was found that protein‐like properties are maintained by using the (1 R ,2 S )‐2‐aminocyclohexanecarboxylic acid building blocks.