Issue 24, 2012

Probing in cellprotein 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.

Graphical abstract: Probing in cell protein structural changes with time-resolved X-ray scattering

Supplementary files

Article information

Article type
Communication
Submitted
16 Feb 2012
Accepted
23 Apr 2012
First published
17 May 2012

Soft Matter, 2012,8, 6434-6437

Probing in cell protein structural changes with time-resolved X-ray scattering

A. Spilotros, M. Levantino, G. Schirò, M. Cammarata, M. Wulff and A. Cupane, Soft Matter, 2012, 8, 6434 DOI: 10.1039/C2SM25676B

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements