Specificity of native-like interhelical hydrophobic contacts in the apomyoglobin intermediate

On exposure to mildly acidic conditions, apomyoglobin forms a partially folded intermediate, I. The A, B, G, and H helices are significantly structured in this equilibrium intermediate, whereas the remainder of the protein is largely unfolded. We report here the effects of mutations at helix pairing...

Täydet tiedot

Bibliografiset tiedot

Julkaisussa:	Proc Natl Acad Sci U S A
Päätekijät:	Kay, Michael S., Ramos, Carlos H. I., Baldwin, Robert L.
Aineistotyyppi:	Artigo
Kieli:	Inglês
Julkaistu:	National Academy of Sciences 1999
Aiheet:	Biological Sciences
Linkit:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC26727/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10051585/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.96.5.2007
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