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A β/γ Motif to Mimic α‐Helical Turns in Proteins
Author(s) -
Rezaei Araghi Raheleh,
Jäckel Christian,
Cölfen Helmut,
Salwiczek Mario,
Völkel Antje,
Wagner Sara C.,
Wieczorek Sebastian,
Baldauf Carsten,
Koksch Beate
Publication year - 2010
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200900700
Subject(s) - motif (music) , coiled coil , chemistry , computational biology , structural motif , amino acid , stereochemistry , computer science , biochemistry , biology , physics , acoustics
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.
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