Research report 2010 - Max Planck Research Unit for Enzymology of Protein Folding
Light-modulated protein structures using chemical modification of the backbone
Authors
Fischer, Gunter
Departments
Enzymologie der Proteinfaltung (Prof. Dr. Gunter Fischer)
Max-Planck-Forschungsstelle für Enzymologie der Proteinfaltung, Halle
Max-Planck-Forschungsstelle für Enzymologie der Proteinfaltung, Halle
Summary
The combination of translational and posttranslational modifications generates structural complexity of proteins. However, a number of problems regarding protein functions escape solution because of the limited repertoire of chemical modification currently available. We have substituted oxygen atoms of an oligopeptide backbone with sulphur or selenium. Photoswitching of the derivatives produced a fraction of molecules representing high energy conformers. Their transient existence allows the evaluation of folding-function relationships on the one-bond level of conformational interconversions.