Protein packing defects “heat up” interfacial water

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 bee...

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Bibliographic Details
Published in:The European physical journal. E, Soft matter and biological physics Soft matter and biological physics, 2013-06, Vol.36 (6), p.62-62, Article 62
Main Authors: Sierra, María Belén, Accordino, Sebastián R., Rodriguez-Fris, J. Ariel, Morini, Marcela A., Appignanesi, Gustavo A., Fernández Stigliano, Ariel
Format: Article
Language:English
Subjects:
Binding Sites
Biological and Medical Physics
Biophysics
Chemistry
Complex Fluids and Microfluidics
Complex Systems
Exact sciences and technology
General and physical chemistry
Hydrogen Bonding
Ligands
Nanotechnology
Physics
Physics and Astronomy
Polymer Sciences
Protein Structure, Tertiary
Proteins - chemistry
Proteins - metabolism
Regular Article
Soft and Granular Matter
Surface physical chemistry
Surfaces and Interfaces
Temperature
Thin Films
Tumor Suppressor Protein p53 - chemistry
Tumor Suppressor Protein p53 - metabolism
Water - chemistry
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Summary: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. Graphical abstract
ISSN:1292-8941
1292-895X
DOI:10.1140/epje/i2013-13062-7