Obtaining detailed structural information about the interactions between amyloid-forming proteins and inhibitors can be extremely difficult. Two-dimensional infrared spectroscopy has now risen to this challenge to show the mapping of protein–protein contact sites in real time.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 12 print issues and online access
$259.00 per year
only $21.58 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
References
Middleton, C. T. et al. Nature Chem. 4, 355–360 (2012).
Goldsbury, C. S. et al. J. Struct.Biol. 119, 17–27 (1997).
Luca, S., Yau, W. M., Leapman, R. & Tycko, R. Biochem. 46, 13505–13522 (2007).
Cao, P., Meng, F., Abedini, A. & Raleigh, D. P. Biochem. 49, 872–881 (2010).
Hamm, P., Lim, M. & Hochstrasser, R. M. J. Phys. Chem. B 102, 6123–6138 (1998).
Cho, M. Two-Dimensional Optical Spectroscopy (CRC Press, 2009)
Waegele, M. M., Culik, R. M. & Gai, F. J. Phys. Chem. Lett. 2, 2598–2609 (2011).
Taskent-Sezgin, H. et al. Angew. Chem. Int. Ed. 49, 7473–7475 (2010).
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Cho, M. Mapping protein–protein contacts. Nature Chem 4, 339–341 (2012). https://doi.org/10.1038/nchem.1336
Published:
Issue Date:
DOI: https://doi.org/10.1038/nchem.1336
This article is cited by
-
Mid-infrared spectroscopy for protein analysis: potential and challenges
Analytical and Bioanalytical Chemistry (2016)