The SFB 1078 kindly invites you to the following colloquium talk:

Prof. Paula Booth

King's College London, UK

Title: Co-translational folding of membrane proteins

Abstract: 

The folding of newly synthesised proteins to their correct structure is essential to attaining functionally normal proteins that are vital to health. The majority of folding research studies artificially-denatured, full-length chains - a situation that is unrepresentative of cellular folding. Although folding is a highly topical area of research, membrane proteins are a particularly understudied class. Nearly all alpha helical membrane proteins fold co-translationally during biosynthesis, as the ribosome is translating mRNA, with insertion being assisted by translocase apparatus. Thus, the proteins fold in the membrane during elongation of the polypeptide chain, and not as full-length chains. We have developed a range of cell-free approaches and tools to probe co-translational folding to enable study of transient intermediates. We have also advanced our studies to native lipid compositions and the study of ribosome nascent chain complexes a strapped intermediates, where different length nascent chains are stalled whilst still attached to the ribosome.