Effect of Aggregation and Molecular Size on the Ice Nucleation Efficiency of Proteins.
Environ Sci Technol
; 58(10): 4594-4605, 2024 Mar 12.
Article
in En
| MEDLINE
| ID: mdl-38408303
ABSTRACT
Aerosol acts as ice-nucleating particles (INPs) by catalyzing the formation of ice crystals in clouds at temperatures above the homogeneous nucleation threshold (-38 °C). In this study, we show that the immersion mode ice nucleation efficiency of the environmentally relevant protein, ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO), occurs at temperatures between -6.8 and -31.6 °C. Further, we suggest that this range is controlled by the RuBisCO concentration and protein aggregation. The warmest median nucleation temperature (-7.9 ± 0.8 °C) was associated with the highest concentration of RuBisCO (2 × 10-1 mg mL-1) and large aggregates with a hydrodynamic diameter of â¼103 nm. We investigated four additional chemically and structurally diverse proteins, plus the tripeptide glutathione, and found that each of them was a less effective INP than RuBisCO. Ice nucleation efficiency of the proteins was independent of the size (molecular weight) for the five proteins investigated in this study. In contrast to previous work, increasing the concentration and degree of aggregation did not universally increase ice nucleation efficiency. RuBisCO was the exception to this generalization, although the underlying molecular mechanism determining why aggregated RuBisCO is such an effective INP remains elusive.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Ribulose-Bisphosphate Carboxylase
/
Ice
Language:
En
Journal:
Environ Sci Technol
Year:
2024
Document type:
Article
Affiliation country:
Estados Unidos