| Literature DB >> 9698544 |
G Mer1, E Kellenberger, J F Lefèvre.
Abstract
It is shown here that the three-dimensional arrangement of the amino acids in an RGDF beta-turn (sequence involved in cell adhesion) resembles that of an alpha-helix with a shuffled RGDF sequence (i.e. RGXFD). A miniprotein 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 beta-turn can thus be mimicked by an alpha-helix. Copyright 1998 Academic PressMesh：
Substances：
Year: 1998 PMID： 9698544 DOI： 10.1006/jmbi.1998.1939
Source DB: PubMed Journal: J Mol Biol ISSN： 0022-2836 Impact factor: 5.469