The C-terminal tails of GroEL and its mitochondrial and chloroplastic homologs adopt polyproline II...
The C-terminal tails of GroEL and its mitochondrial and chloroplastic homologs adopt polyproline II helices
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Publisher
Cold Spring Harbor Laboratory
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Language
English
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Cold Spring Harbor Laboratory
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Contents
The chaperonin GroEL and its mitochondrial and chloroplastic homologs mHsp60 and Cpn60 are large barrel-like oligomeric proteins. Chaperonins facilitate folding by isolating nascent chains in their hollow interior and undergoing conformational transitions driven by ATP hydrolysis. Due to their vital importance, the structure of GroEL and its homolo...
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Full title
The C-terminal tails of GroEL and its mitochondrial and chloroplastic homologs adopt polyproline II helices
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TN_cdi_biorxiv_primary_2024_05_27_596059
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_biorxiv_primary_2024_05_27_596059
Other Identifiers
E-ISSN
2692-8205
DOI
10.1101/2024.05.27.596059
