par Gilis, Dimitri 
;Dehouck, Yves ;Rooman, Marianne
Référence Amyloid and Amyloidosis, CRC Press, page (3-5)
Publication Publié, 2004-01
;Dehouck, Yves ;Rooman, Marianne Référence Amyloid and Amyloidosis, CRC Press, page (3-5)
Publication Publié, 2004-01
Partie d'ouvrage collectif
| Résumé : | Proteins are biopolymers that present the particularity to adopt a specific tridimensional structure (3D) dictated by their amino acid sequence. As they are generally only active in their folded form, it is important to get information about their 3D structure, whether by in vitro or in silico means. It has often been assumed that the 3D structure is unique, but the recent discovery that profound conformational changes may affect isolated proteins in native or non-native environments, or proteins interacting with molecules unrelated to their activity, has shaken this postulate. These conformational changes are at the basis of the so-called conformational diseases (1, 2), such as the Creutzfeld-Jakob disease provoked by the misfolding of the prion protein or those caused by serpin polymerization (3). We briefly survey the general techniques for predicting the 3D structure of a protein from its sequence, and present the in silico design of amino acid mutations that modify the misfolding propensities of AL-antitrypsin, a disease-causing serpin. |
