The shock of the old: hydrodynamics for the masses.
Hydrodynamic techniques such as analytical ultracentrifugation can provide key information about subunit stoichiometry and interaction strengths of protein-nucleic acid interactions. Analysis is complicated by (i) the need for low concentrations in order to observe both free and bound species and (ii) thermodynamic non-ideality. With the introduction of fluorescence optics, we are able to obtain data at lower concentrations, and improved understanding of the statistical thermodynamics of macromolecular solutions has allowed non-ideality to be accurately assigned. With these developments, it is possible now to assay protein-nucleic acid interactions at concentrations typically used in molecular biology assays.
Scott
David J
DJ
National Centre for Macromolecular Hydrodynamics, School of Biosciences, University of Nottingham, Sutton Bonington Campus, Leicestershire, UK. dj.scott@nottingham.ac.uk
D009696:Nucleic Acids / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D011506:Proteins / Q000235:genetics / Q000378:metabolism; D013816:Thermodynamics; D014461:Ultracentrifugation; D014867:Water / Q000737:chemistry*
D009696:Nucleic Acids; D011506:Proteins; D014867:Water