Abstract
It is shown here that the three-dimensional arrangement of the amino acids in an RGDF β-turn (sequence involved in cell adhesion) resembles that of an α-helix with a shuffled RGDF sequence (i.e. RGXFD). A mini-protein was designed and constructed which arranges the RGXFD sequence into a well defined helical conformation. The designed protein is bioactive and folds into the desired structure as assessed by nuclear magnetic resonance spectroscopy. The recognition process mediated by a β-turn can thus be mimicked by an α-helix.
Original language | English (US) |
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Pages (from-to) | 235-240 |
Number of pages | 6 |
Journal | Journal of Molecular Biology |
Volume | 281 |
Issue number | 2 |
DOIs | |
State | Published - Aug 14 1998 |
Keywords
- NMR spectroscopy
- Protein design
- Protein folding
- α-helix
- β-turn
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology