| Popis: |
Biochemical and biophysical analyses of reversible associations may be reduced to a few fundamental pieces of information. One is the degree to which the complexes are formed (vs. disassembled) in any particular setting (concentrations, temperature, salts, etc.) Another is the docking geometry and conformation of such complexes. The latter information can be gleaned from structural techniques such as X-ray crystallography solution, NMR spectroscopy, SANS, or SAXS (or in some cases, cryo-EM studies), but many of those detailed methods are performed in conditions that change the equilibria we mean to study in the first place; i.e., either concentrations or temperatures are outside of the physiologically interesting regime. The fact that interesting and relevant structures still emerge is a tribute to artistry in those methods and an indication that many complexes are hardy and long-lived. It would be advantageous, however, to also work with techniques that are capable of working on low concentration samples (needed to assess the stoichiometry of tight interactions) and that are sensitive to short-lived, flexible, fragile, or sparsely populated complexes. |
