On the engulfment of antifreeze proteins by ice.
Proc Natl Acad Sci U S A
; 121(24): e2320205121, 2024 Jun 11.
Article
en En
| MEDLINE
| ID: mdl-38833468
ABSTRACT
Antifreeze proteins (AFPs) are remarkable biomolecules that suppress ice formation at trace concentrations. To inhibit ice growth, AFPs must not only bind to ice crystals, but also resist engulfment by ice. The highest supercooling, [Formula see text], for which AFPs are able to resist engulfment is widely believed to scale as the inverse of the separation, [Formula see text], between bound AFPs, whereas its dependence on the molecular characteristics of the AFP remains poorly understood. By using specialized molecular simulations and interfacial thermodynamics, here, we show that in contrast with conventional wisdom, [Formula see text] scales as [Formula see text] and not as [Formula see text]. We further show that [Formula see text] is proportional to AFP size and that diverse naturally occurring AFPs are optimal at resisting engulfment by ice. By facilitating the development of AFP structure-function relationships, we hope that our findings will pave the way for the rational design of AFPs.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Proteínas Anticongelantes
/
Hielo
Límite:
Animals
Idioma:
En
Revista:
Proc Natl Acad Sci U S A
Año:
2024
Tipo del documento:
Article