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Imaging Protein Fibers at the Nanoscale and In Situ.

Bella, A; Shaw, M; De Santis, E; Ryadnov, MG; (2018) Imaging Protein Fibers at the Nanoscale and In Situ. Methods in Molecular Biology , 1777 pp. 83-100. 10.1007/978-1-4939-7811-3_4. Green open access

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Abstract

Protein self-assembly offers a rich repertoire of tools and technologies. However, despite significant progress in this area, a deterministic measure of the phenomenon, which might lead to predictable relationships between protein components, assembly mechanisms, and ultimately function, is lacking. Often the challenge relates to the choice of the most informative and precise measurements that can link the chemistry of the building blocks with the resulting assembly, ideally in situ and in real time. Using the example of protein fibrillogenesis-a self-assembly process fundamental to nearly every aspect of biological organization, from viral assembly to tissue restoration-this chapter demonstrates how protein self-assembly can be visually and precisely measured while providing measurement protocols applicable to other self-assembly systems.

Type: Article
Title: Imaging Protein Fibers at the Nanoscale and In Situ.
Location: United States
Open access status: An open access version is available from UCL Discovery
DOI: 10.1007/978-1-4939-7811-3_4
Publisher version: https://doi.org/10.1007/978-1-4939-7811-3_4
Language: English
Additional information: This version is the author accepted manuscript. For information on re-use, please refer to the publisher’s terms and conditions.
Keywords: Molecular self-assembly, Nanometrology, Nanoscale biophysics, Protein fibrillogenesis, Real-time imaging, Super-resolution microscopy
UCL classification: UCL
UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > UCL BEAMS
UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Engineering Science
UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Engineering Science > Dept of Computer Science
URI: https://discovery.ucl.ac.uk/id/eprint/10053592
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