Unknown

Dataset Information

0

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


ABSTRACT: 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.

SUBMITTER: Cammarata M 

PROVIDER: S-EPMC3159148 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Cammarata Marco M   Levantino Matteo M   Schotte Friedrich F   Anfinrud Philip A PA   Ewald Friederike F   Choi Jungkweon J   Cupane Antonio A   Wulff Michael M   Ihee Hyotcherl H  

Nature methods 20080921 10


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 int  ...[more]

Similar Datasets

| S-EPMC4659713 | biostudies-literature
| S-EPMC7511240 | biostudies-literature
| S-EPMC6274816 | biostudies-literature
| S-EPMC4104061 | biostudies-literature
| S-EPMC6533112 | biostudies-literature
| S-EPMC3057577 | biostudies-literature
| S-EPMC6041135 | biostudies-literature
| S-EPMC5336379 | biostudies-literature
| S-EPMC6211537 | biostudies-literature
| S-EPMC4833754 | biostudies-literature