Protein folding, animation. In order to function correctly proteins have to adopt the correct three dimensional structure. This is done by folding. In some proteins, disulphide bridges (S-S) form between adjacent cysteine residues during folding. The addition of urea and mercaptoethanol to the protein's environment breaks these bridges, reducing them to two SH groups, and causes the denaturing (unfolding) of the protein. When urea and mercaptoethanol are removed the SH groups oxidise spontaneously to reform the disulphide bridges and the protein refolds. | |
Licence : | Droits gérés |
Crédit : | Science Photo Library / Biocosmos / Francis Leroy & Georges Lambert |
Model Release : | Non requis |
Durée : | 31 Secondes |
Aspect ratio : | 16/9 |
Restrictions : | - |