Abstract:
:To examine stabilizing effects of the base pair interaction on a protein scaffold, various peptides with L-α-amino acids bearing a nucleobase in the side chain (nucleobase amino acids; NBAs) were designed based on a G-peptide β-hairpin structure, and their conformational properties were investigated by circular dichroism and NMR spectroscopy. Thermodynamic analyses based on the chemical shifts showed that adenine-thymine pairing in a diagonal fashion at positions 4 and 15 (2AT) enhanced thermal stability of the peptide conformation by more than 30 K as compared with the wild-type G-peptide. In NOESY spectrum, not only numerous nonadjacent crosspeaks but also long-range crosspeaks between the nucleobases were observed in some peptides with the base pairing. NMR structure calculations of the 2AT peptide confirmed that cross-strand pairing of the nucleobases occurs on the well-defined β-hairpin structure as designed. Taken together, the base pairing in an appropriate position and orientation facilitates folding and stabilization of a native-like β-hairpin structure.
journal_name
Biopolymersjournal_title
Biopolymersauthors
Uozumi R,Takahashi T,Yamazaki T,Granholm V,Mihara Hdoi
10.1002/bip.21464subject
Has Abstractpub_date
2010-01-01 00:00:00pages
830-42issue
6eissn
0006-3525issn
1097-0282journal_volume
94pub_type
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