Cargando…
How do chaperonins fold protein?
Protein folding is a biological process that is essential for the proper functioning of proteins in all living organisms. In cells, many proteins require the assistance of molecular chaperones for their folding. Chaperonins belong to a class of molecular chaperones that have been extensively studied...
Autor principal: | Motojima, Fumihiro |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Biophysical Society of Japan (BSJ)
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4736790/ https://www.ncbi.nlm.nih.gov/pubmed/27493521 http://dx.doi.org/10.2142/biophysics.11.93 |
Ejemplares similares
-
Chaperonin facilitates protein folding by avoiding initial polypeptide collapse
por: Motojima, Fumihiro, et al.
Publicado: (2018) -
Chaperonin-mediated folding of actin and tubulin
Publicado: (1996) -
Mechanistic insights into protein folding by the eukaryotic chaperonin complex CCT
por: Smith, Theresa M., et al.
Publicado: (2022) -
Friends in need: How chaperonins recognize and remodel proteins that require folding assistance
por: Stan, George, et al.
Publicado: (2022) -
Functional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding
por: Kabir, M. Anaul, et al.
Publicado: (2011)