Effect of shortening Ω-loop D on 3D domain swapping in cytochrome c

Clicks: 33
ID: 325083
2026
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This article has not been analysed, so there is no overall score — reader engagement is measured and shown alongside.
AI Quality Assessment
Not analyzed
Readership in this journal
Emerging

Ranked #732 of 820 articles by views in phytochemistry letters

Most read Least read

Bar heights use a square-root scale. Only the 120 most-read articles are drawn; the journal has 820 in total.

Mint this article as an NFT
Not yet minted

Create a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.

5 SUSD one-off · no wallet required
Abstract
Abstract Three-dimensional domain swapping (3D-DS) properties of wild-type human cyt c and its variants, in which one to five residues were deleted from Ω-loop D, were investigated. The cyt c dimer stability generally decreased as more amino acids were deleted from Ω-loop D. However, the del82-85 dimer exhibited a relatively small dissociation rate constant and hydrodynamic size, indicating that protein–protein interactions between the functional globular units play a crucial role in determining the stability of the 3D-DS dimer.
Reference Key
openalex_W7203648386 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors
Journal phytochemistry letters
Year 2026
DOI
10.1093/chemle/upag163
URL
Keywords Keywords not found

Citations

No citations found. To add a citation, contact the admin at info@scimatic.org

No comments yet. Be the first to comment on this article.