Ontology highlight
ABSTRACT:
SUBMITTER: Clancy B
PROVIDER: S-EPMC6697465 | biostudies-literature | 2019 Aug
REPOSITORIES: biostudies-literature
Clancy Bason B Moree Ben B Salafsky Joshua J
Biophysical journal 20190711 3
Proteins are inherently dynamic, flexible molecules that execute precise conformational changes to perform their functions, but existing techniques to directly measure relevant structural changes in solution at room temperature remain limited. Here, we demonstrate a structural technique using second-harmonic generation and two-photon fluorescence under single-laser excitation to map both the mean angular orientation and the distribution width of a probe at various sites throughout the protein wi ...[more]