Investigating protein structural changes inside the cell is a major goal in molecular biology. Here we show that time-resolved wide-angle X-ray scattering is a valuable tool for this purpose. Hemoglobin has been chosen as a model system and its tertiary and quaternary conformational changes following laser flash-photolysis have been tracked in intact red blood cells with nanosecond time resolution.
title = "Probing in cell protein structural changes with time-resolved X-ray scattering",
abstract = "Investigating protein structural changes inside the cell is a major goal in molecular biology. Here we show that time-resolved wide-angle X-ray scattering is a valuable tool for this purpose. Hemoglobin has been chosen as a model system and its tertiary and quaternary conformational changes following laser flash-photolysis have been tracked in intact red blood cells with nanosecond time resolution.",
author = "Giorgio Schiro' and Antonio Cupane and Matteo Levantino and Michael Wulff and Marco Cammarata and Alessandro Spilotros",
year = "2012",
language = "English",
volume = "8",
pages = "6434--6437",
journal = "Soft Matter",
issn = "1744-683X",
publisher = "Royal Society of Chemistry",
}
TY - JOUR
T1 - Probing in cell protein structural changes with time-resolved X-ray scattering
AU - Schiro', Giorgio
AU - Cupane, Antonio
AU - Levantino, Matteo
AU - Wulff, Michael
AU - Cammarata, Marco
AU - Spilotros, Alessandro
PY - 2012
Y1 - 2012
N2 - Investigating protein structural changes inside the cell is a major goal in molecular biology. Here we show that time-resolved wide-angle X-ray scattering is a valuable tool for this purpose. Hemoglobin has been chosen as a model system and its tertiary and quaternary conformational changes following laser flash-photolysis have been tracked in intact red blood cells with nanosecond time resolution.
AB - Investigating protein structural changes inside the cell is a major goal in molecular biology. Here we show that time-resolved wide-angle X-ray scattering is a valuable tool for this purpose. Hemoglobin has been chosen as a model system and its tertiary and quaternary conformational changes following laser flash-photolysis have been tracked in intact red blood cells with nanosecond time resolution.
UR - http://hdl.handle.net/10447/63231
UR - http://pubs.rsc.org/en/content/articlelanding/2012/sm/c2sm25676b