Exploration of tropocollagen unwinding by cathepsin K dimer with chondroitin 4-sulphate through microsecond timescale molecular dynamics
Mengyi Shan, Yue Wu, Chen Jiang, Jing Chen, Gang Cheng, Lu-Ping Qin · 2026
Read Exploration of tropocollagen unwinding by cathepsin K dimer with chondroitin 4-sulphate through microsecond timescale molecular dynamics by Mengyi Shan, Yue Wu, Chen Jiang, Jing Chen, Gang Cheng, Lu-Ping Qin (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/PMC13410547.txt.
Description
Mengyi Shan and colleagues simulate in 2026 how an enzyme unravels collagen, the tough protein of bone and skin. The enzyme, cathepsin K, is unusual: with help from a sugar-like partner it can unwind collagen's triple helix and cut it up. Blocking it is a hope for bone disease drugs, yet the unwinding steps were unclear.
Computer runs lasting millionths of a second followed the enzyme pair, a collagen segment, and the sugar partner in water. Unwinding began when six key links between the collagen strands broke. The sugar partner curved across both enzyme and collagen, holding the trio steady. Two enzyme spots helped pry strands apart, offering targets for future drug design.
Catalog record
| CREATOR | Mengyi Shan, Yue Wu, Chen Jiang, Jing Chen, Gang Cheng, Lu-Ping Qin |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 41 KB |
| LICENSE | https://creativecommons.org/licenses/by/4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |