IAM   02674
INSTITUTO ARGENTINO DE MATEMATICA ALBERTO CALDERON
Unidad Ejecutora - UE
artículos
Título:
Protein packing defects ``heat up'' interfacial
Autor/es:
SIERRA, MARÍA BELÉN; ACCORDINO, SEBASTIÁN ROBERTO; RODRIGUEZ FRIS, JORGE ARIEL; MORINI, MARCELA ANA; APPIGNANESI, GUSTAVO ADRIÁN; FERNÁNDEZ, ARIEL
Revista:
The European Physical Journal E
Editorial:
EDP Sciences
Referencias:
Año: 2013 vol. 36 p. 1 - 1
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.