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Literature summary for 2.1.1.297 extracted from

  • Kemp, G.; Kudva, R.; de la Rosa, A.; von Heijne, G.
    Force-profile analysis of the cotranslational folding of HemK and filamin domains comparison of biochemical and biophysical folding assays (2019), J. Mol. Biol., 431, 1308-1314 .
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
gene HEMK1, recombinant expression of isolated N-terminal domain and of truncated mutants in Escherichia coli, cotranslational folding of the HemK N-terminal domain Homo sapiens

Protein Variants

Protein Variants Comment Organism
L27A/L28A site-directed mutagenesis Homo sapiens
L28A site-directed mutagenesis, the L28A mutation reduces the in vitro denaturation temperature of HemK-N-terminal domain from 50°C to 30°C Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9Y5R4
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-

Synonyms

Synonyms Comment Organism
HemK
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Homo sapiens
Hemk1
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Homo sapiens

General Information

General Information Comment Organism
additional information the cotranslational folding of two small protein domains of different folds - the alpha-helical N-terminal domain of HemK and the beta-rich FLN5 filamin domain - by measuring the force that the folding protein exerts on the nascent chain when located in different parts of the ribosome exit tunnel (force-profile analysis, or FPA), allowing us to compare FPA to three other techniques currently used to study cotranslational folding: real-time FRET, photoinduced electron transfer, and NMR, method evaluation, overview Homo sapiens