Structural insight into co-translational membrane protein folding.
Biochim Biophys Acta Biomembr
; 1862(1): 183019, 2020 01 01.
Article
in En
| MEDLINE
| ID: mdl-31302079
ABSTRACT
Membrane protein folding studies lag behind those of water-soluble proteins due to immense difficulties of experimental study, resulting from the need to provide a hydrophobic lipid-bilayer environment when investigated in vitro. A sound understanding of folding mechanisms is important for membrane proteins as they contribute to a third of the proteome and are frequently associated with disease when mutated and/or misfolded. Membrane proteins largely consist of α-helical, hydrophobic transmembrane domains, which insert into the membrane, often using the SecYEG/Sec61 translocase system. This mini-review highlights recent advances in techniques that can further our understanding of co-translational folding and notably, the structure and insertion of nascent chains as they emerge from translating ribosomes. This article is part of a Special Issue entitled Molecular biophysics of membranes and membrane proteins.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Protein Folding
/
Protein Translocation Systems
/
Membrane Proteins
Limits:
Animals
/
Humans
Language:
En
Journal:
Biochim Biophys Acta Biomembr
Year:
2020
Document type:
Article
Affiliation country: