Conferment of folding ability to a naturally unfolded apocytochrome c through introduction of hydrophobic amino acid residues.

doi:10.1021/bi101646m

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Article

Conferment of folding ability to a naturally unfolded apocytochrome c through introduction of hydrophobic amino acid residues.

Biochemistry - 29 Mar 2011

Yamanaka Masaru, Masanari Misa, Sambongi Yoshihiro

Abstract excerpt

Hyperthermophilic Aquifex aeolicus cytochrome c(555) (AA c(555)) exceptionally folds even in the apo state, unlike general cytochromes c including mesophilic Pseudomonas aeruginosa cytochrome c(551) (PA c(551)), which is structurally homologous to AA c(555) in the holo state. Here we hypothesized that the exceptional apo AA c(555) folding can be attributed to nine hydrophobic amino acid residues and proved this...

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PMID: 21329369
DOI: 10.1021/bi101646m

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.