In cell-free interaction studies, Tβ4 engaged in multiple weak, transient and fuzzy interactions with partners without adopting stable folded structures.
In plain wordsIn lab tests, Tβ4 formed many weak, short-lived contacts with its partner proteins without taking a fixed shape.
- Peptide
- Thymosin beta-4 (human)
- Outcome
- Not applicableTβ4 binding interactions
- Study
n: not reported in source
- Outcome group
- Receptor activity and mechanism · Pharmacology
- Studied dose
- Dose not stated
Source sentences
Unexpectedly, we found that Tβ4 engages in multiple weak, transient, and fuzzy interactions, i.e., it is capable of mediating distinct yet specific interactions without adapting stable folded structures.
1 context sentence(design, population, supporting numbers)
Because Tβ4 is mostly disordered, and its 4 described partners are structurally unrelated (the CTD of stabilin-2 is actually fully disordered), it occurred to us that this system might be ideal to characterize the structural adaptability and ensuing moonlighting functions of IDPs.