Relating protein crystal structure to ligand-binding thermodynamics

Research output: Contribution to journalArticlepeer-review

Abstract

An important interface between biophysical chemistry and biological crystal structures involves whether it is possible to relate experimental calorimetry measurements of protein ligand binding to 3D structures. This has proved to be challenging. The probes of the structure of matter, namely X-rays, neutrons and electrons, have challenges of one type or another in their use. This article focuses on saccharide binding to lectins as a theme, yet after 25 years or so it is still a work in progress to connect 3D structure to binding energies. Whilst this study involved one type of protein (lectins) and one class of ligand (monosaccharides), i.e. it was specific, it was of general importance, as measured for instance by its wide impact. The impetus for writing this update now, as a Scientific Comment, is that a breakthrough in neutron crystal structure determinations of saccharide-bound lectins has been achieved. It is suggested here that this new research from neutron protein crystallography could improve, i.e. reduce, the errors in the estimated binding energies.

Original languageEnglish
Pages (from-to)403-407
Number of pages5
JournalActa Crystallographica. Section F: Structural Biology and Crystallization Communications
Volume78
Issue numberPt 12
DOIs
Publication statusPublished - 1 Dec 2022

Keywords

  • Ligands
  • Crystallography, X-Ray
  • Thermodynamics
  • Lectins
  • Calorimetry

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