Abstract
Single-molecule biophysical tools have developed in the past two decades from jaw-dropping attractions to essential laboratory tools. In recent years, these methods have been applied to the exploration of the structure, mechanics, and mechanically driven conformational changes of amyloidogenic protein systems as well. Amyloidogenic proteins are a rich and diverse group of molecules capable of forming amyloid fibrils, and many of them are implicated in severe degenerative diseases. Because many of the diseases cause not only health problems but societal burden as well, experimental research aiming at obtaining quicker and more precise diagnosis, a better understanding of the molecular mechanisms, and more efficient therapies has ever been intensifying. In spite of seeing greater structural detail in amyloid fibrils, the intrafibrillar dynamics, the nature of the structural changes related to the amyloidogenic transition, and the role that mechanical properties might play are still not understood well. Single-molecule methods offer a unique insight into the behavior of amyloidogenic proteins and amyloid fibrils. This chapter focuses primarily on single-molecule mechanics approaches. Single-molecule methods are described and the adaptation of the techniques in the investigation of a number of amyloidogenic systems is discussed.
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Acknowledgments
This work was supported by grants from the Hungarian Science Foundation (OTKA K73256 and K84133) and the Hungarian National Development Agency (TAMOP-4.2.1.B-09/1/KMR-2010-0001).
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Kellermayer, M.S.Z., Karsai, Á., Murvai, Ü., Erdélyi-Bótor, S., Kardos, J., Pires, R.H. (2012). Single-Molecule Studies of Amyloidogenic Proteins. In: Oberhauser, A. (eds) Single-molecule Studies of Proteins. Biophysics for the Life Sciences, vol 2. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-4921-8_7
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