Synonymous and non‐synonymous codon substitutions can alleviate dependence on GroEL for folding

The Escherichia coli GroEL/ES chaperonin system facilitates protein folding in an ATP‐driven manner. There are

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Bibliographic Details
Published in:Protein science 2024-08, Vol.33 (8), p.e5087-n/a
Main Authors: Reingewertz, Tali Haviv, Ben‐Maimon, Miki, Zafrir, Zohar, Tuller, Tamir, Horovitz, Amnon
Format: Article
Language:English
Subjects:
Animals
Chaperonin 60 - chemistry
Chaperonin 60 - genetics
Chaperonin 60 - metabolism
chaperonins
Clients
Codon - genetics
Codon - metabolism
codon usage
Dihydrofolate reductase
E coli
Escherichia coli - genetics
Escherichia coli - metabolism
Folding
GroEL
Mice
Protein Folding
Proteins
random mutagenesis
Reductases
Silent Mutation
Tetrahydrofolate Dehydrogenase - chemistry
Tetrahydrofolate Dehydrogenase - genetics
Tetrahydrofolate Dehydrogenase - metabolism
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Description
Summary:The Escherichia coli GroEL/ES chaperonin system facilitates protein folding in an ATP‐driven manner. There are
ISSN:0961-8368
1469-896X
1469-896X
DOI:10.1002/pro.5087