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Small-angle Solution Scattering of Proteins

Issue: Vol.6, No.2 - April 2007

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Article Type: Manuscript

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  1. Ruth Prassl
    Institute of Biophysics and X-Ray Structure Research, Austrian Academy of Sciences
  2. Michal Hammel
  3. Peter Laggner

In structural proteomics it has become increasingly evident that the structure of proteins in solution and under the influence of different, specific or non-specific additives, is often different from the crystal structure. This feature might exert fundamental functional influence on e.g. membrane association, ligand or receptor binding, enzyme activity or immune response. At the same time, the methods of small angle scattering have reached a state of development, both in hard- and software, where the routine application in the proteomics laboratory has become feasible. Hence, questions such as oligomerization or conformational changes induced by different environmental conditions can be answered. The impact of small molecules, ligands, lipids or drugs on the overall conformation of the protein can be visualized. Moreover, a rational combination of small angle scattering data with X-ray crystallographic data, molecular dynamics and bioinformatics offers to structural biologists the opportunity to assemble individual protein modules in a bottom-up strategy to get information on complex macromolecular structures. Thus, most recent advances in instrumentation and methodology of small angle scattering have opened important new ways for molecular structure determination. In this mini-review we report on the rapid increasing progress achieved in the field of small angle scattering techniques and outline some problems which can be addressed by solution scattering. We briefly review the strengths and limitations of the methodology and finally discuss some of our recent results showing how small angle scattering can be used to obtain essential information on protein structure in solution and how conclusions on the functional behavior of a protein can be drawn based on solution structural data.

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