ArticleJournal of inorganic biochemistry2016
Cytochrome unfolding pathways from computational analysis of crystal structures.
Article in Journal of inorganic biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Unfolding cytochromes c-bJournal of inorganic biochemistry · 2020Article
- Funneled angle landscapes for helical proteins.Journal of inorganic biochemistry · 2020Article
- Structural stabilities of calcium proteins: Human intelectin-1 and frog lectin XEEL.Journal of inorganic biochemistry · 2018Article
- Relaxation of structural constraints during Amicyanin unfolding.Journal of inorganic biochemistry · 2018Article
- Structural Stability of Intelectin-1.The journal of physical chemistry. B · 2016Article
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3 authors.
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Abstract
We have developed a model to study the role of geometrical factors in influencing the early stages of unfolding in three cytochromes: cyt c', cyt c-b562 and cyt c. Each stage in unfolding is quantified by the spatial extension λ̂i of n-residue segments, and by their angular extension 〈βn〉. Similarities and differences between and among the three cytochromes in the unfolding of helical and non-helical regions can be determined by analyzing the data for each signature separately. Definite conclusions can be drawn when spatial and angular changes are considered in tandem. To facilitate comparisons, we present graphical portraits of the three cytochromes at the same stage of unfolding, and in relation to their native state structures. We also display specific segments at different stages of unfolding to illustrate differences in stability of defined domains thereby allowing us to make specific predictions on the unfolding of corresponding internal and terminal helices in cyt c' and cyt c-b562. Our work accords with an earlier experimental report on the presence and persistence of a hydrophobic core in cyt c.
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