Effect of shortening Ω-loop D on 3D domain swapping in cytochrome c
Clicks: 5
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.
Reader Engagement
Emerging Content
1.2
/100
5 views
3 readers
AI Quality Assessment
Not analyzed
Readership in this journal
EmergingRanked #727 of 788 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 788 in total.
Mint this article as an NFT
Not yet mintedCreate 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 | Kotori Ota, Myriam Mahoudi, Tsuyoshi Mashima, Shun Hirota |
| 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
Comments
No comments yet. Be the first to comment on this article.