Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering

• Published in: Nature methods Vol. 5; no. 10; pp. 881 - 886
• Main Authors: Ewald, Friederike, Anfinrud, Philip A, Cammarata, Marco, Cupane, Antonio, Wulff, Michael, Levantino, Matteo, Ihee, Hyotcherl, Schotte, Friedrich, Choi, Jungkweon
• Format: Journal Article
• Language: English
• Published: United States Nature Publishing Group 01.10.2008
• Subjects: Conformational analysis; Crystal structure; Crystallography, X-Ray; Cytochromes c - chemistry; Hemoglobins - chemistry; Molecular dynamics; Myoglobin - chemistry; Nuclear magnetic resonance; Protein Conformation; Protein folding; Proteins; Proteomics; Research methodology; Scattering, Radiation; Sensitivity and Specificity; Structure; X-ray spectroscopy; X-Rays; South Korea
• ISSN: 1548-7091; 1548-7105
• DOI: 10.1038/nmeth.1255

We demonstrate tracking of protein structural changes with time-resolved wide-angle X-ray scattering (TR-WAXS) with nanosecond time resolution. We investigated the tertiary and quaternary conformational changes of human hemoglobin under nearly physiological conditions triggered by laser-induced ligand photolysis. We also report data on optically induced tertiary relaxations of myoglobin and refolding of cytochrome c to illustrate the wide applicability of the technique. By providing insights into the structural dynamics of proteins functioning in their natural environment, TR-WAXS complements and extends results obtained with time-resolved optical spectroscopy and X-ray crystallography.