Proteinen tolestura tunel erribosomikoan

  1. Sara M-Alicante 1
  2. Arantza Muguruza-Montero 1
  3. Oscar R. Ballesteros 1
  4. Ane Metola 2
  5. Janire Urrutia 1
  6. Alvaro Villarroel 1
  7. Eider Nuñez 1
  1. 1 Universidad Politécnica de Valencia

    Universidad Politécnica de Valencia

    Valencia, España


  2. 2 Stockholm University

    Stockholm University

    Estocolmo, Suecia


Ekaia: Euskal Herriko Unibertsitateko zientzi eta teknologi aldizkaria

ISSN: 0214-9001

Year of publication: 2023

Issue: 43

Pages: 101-116

Type: Article

DOI: 10.1387/EKAIA.23624 DIALNET GOOGLE SCHOLAR lock_openOpen access editor

More publications in: Ekaia: Euskal Herriko Unibertsitateko zientzi eta teknologi aldizkaria


Proteins are synthesised as linear polymers and must fold into their native three-dimensional structure to perform various functions in the cell. Understanding protein folding is crucial because protein misfolding is at the origin of several neurodegenerative diseases. Protein folding can start cotranslationally, i.e. when the emerging peptide is still asso-ciated with the ribosome. Indeed, it has been shown that more than one third of the cell’s proteins fold in the limited space of the ribosome tunnel. Increasing evidence suggests that the ribosome plays a critical role in protein folding. The ribosome can facilitate protein compaction, cause the creation of non-visible media in solution or delay the onset of folding. However, the study of cotranslational folding presents serious difficulties, mainly due to the limitations of the different current techniques. Hence, most studies on protein folding are based on proteins in solution, which are carried out by unfolding and refolding the protein, without taking into account the role of the ribosome in this process. In this article, we summarised the techniques developed in recent years for the study of cotranslational protein folding.