INVESTIGADORES
FERNANDEZ Ariel
artículos
Título:
Protein packing defects heat up interfacial water
Autor/es:
MARIA BELEN SIERRA; SEBASTIAN ACCORDINO; ARIEL RODRIGUEZ-FRIS; MARCELA MORINI; GUSTAVO APPIGNANESI; ARIEL FERNANDEZ STIGLIANO
Revista:
European Physical Journal E
Editorial:
Springer-Verlag
Referencias:
Año: 2013 vol. 36 p. 62 - 62
ISSN:
1292-8941
Resumen:
Ligands must displace water molecules from their corresponding protein surface binding site
during association. Thus, protein binding sites are expected to be surrounded by non-tightly-bound, easily
removable water molecules. In turn, the existence of packing defects at protein binding sites has been also
established. At such structural motifs, named dehydrons, the protein backbone is exposed to the solvent
since the intramolecular interactions are incompletely wrapped by non-polar groups. Hence, dehydrons are
sticky since they depend on additional intermolecular wrapping in order to properly protect the structure
from water attack. Thus, a picture of protein binding is emerging wherein binding sites should be both
dehydrons rich and surrounded by easily removable water. In this work we shall indeed confirm such a
link between structure and dynamics by showing the existence of a firm correlation between the degree of
underwrapping of the protein chain and the mobility of the corresponding hydration water molecules. In
other words, we shall show that protein packing defects promote their local dehydration, thus producing
a region of ?hot? interfacial water which might be easily removed by a ligand upon association.