Neutron spectroscopy on protein solutions employing backscattering with an increased energy range

Research output: Contribution to journalArticle


Novel cold neutron backscattering spectrometers contribute substantially to the understanding of the diffusive dynamics of proteins in dense aqueous suspensions. Such suspensions are fundamentally interesting for instance in terms of the so-called macromolecular crowding, protein cluster formation, gelation, and self-assembly. Notably, backscattering spectrometers with the highest flux can simultaneously access the center-of-mass diffusion of the proteins and the superimposed internal molecular diffusive motions. The nearly complete absence of protein-protein collisions on the accessible nanosecond observation time scale even in dense protein suspensions implies that neutron backscattering accesses the so-called short-time limit for the center-of-mass diffusion. This limit is particularly interesting in terms of a theoretical understanding by concepts from colloid physics. Here we briefly review recent progress in studying protein dynamics achieved with the latest generation of backscattering spectrometers. We illustrate this progress by the first data from a protein solution using the backscattering-and-time-of-flight option BATS on IN16B at the ILL and we outline future perspectives.


  • Christian Beck
  • Markus Appel
  • Marco Grimaldo
  • Felix Roosen-Runge
  • Fajun Zhang
  • Bernhard Frick
  • Frank Schreiber
  • Tilo Seydel
External organisations
  • Institut Laue Langevin
  • University of Tübingen
  • Friedrich-Alexander University Erlangen-Nürnberg
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Condensed Matter Physics


  • Aqueous protein solutions, Cold neutron backscattering, Self-diffusion
Original languageEnglish
Pages (from-to)31-35
Number of pages5
JournalPhysica B: Condensed Matter
Publication statusPublished - 2019
Publication categoryResearch