Measuring Protein Structure and Stability of Protein–Nanoparticle Systems with Synchrotron Radiation Circular Dichroism-Reference-Cited by-同舟云学术

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Measuring Protein Structure and Stability of Protein–Nanoparticle Systems with Synchrotron Radiation Circular Dichroism

Published:2011-09-28 Issue:10 Volume:11 Page:4480-4484
ISSN:1530-6984
Container-title:Nano Letters
language:en
Short-container-title:Nano Lett.

Author:

Laera Stefania¹,Ceccone Giacomo¹,Rossi Francois¹,Gilliland Douglas¹,Hussain Rohanah²,Siligardi Giuliano²³,Calzolai Luigi¹

Affiliation:

1. European Commission, Joint Research Centre, Institute for Health and Consumer Protection I-21027, Ispra (VA), Italy

2. Diamond Light Source, Diamond House, Chilton, Didcot, OX11 0DE, U.K.

3. School of Biological Sciences, University of Liverpool, L69 7ZX, U.K.

Publisher

American Chemical Society (ACS)

Subject

Mechanical Engineering,Condensed Matter Physics,General Materials Science,General Chemistry,Bioengineering

Link

https://pubs.acs.org/doi/pdf/10.1021/nl202909s

Reference17 articles.

1. Understanding biophysicochemical interactions at the nano–bio interface

2. Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts

3. Nanoparticle-induced unfolding of fibrinogen promotes Mac-1 receptor activation and inflammation

4. Protein−Nanoparticle Interaction: Identification of the Ubiquitin−Gold Nanoparticle Interaction Site

5. Circular Dichroism and the Conformational Analysis of Biomolecules

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