Abstract
A common feature of molecular chaperones is their ability to recognize hydrophobic surfaces of unfolded proteins to which they can bind, and thus, stabilize unfolded polypeptides at various levels of conformational compactness (1, 2). Depending on the substrate, different chaperone systems are required to allow folding to the native state. Some proteins fold with high yields in a chaperone-unassisted reaction (3, 4) whereas other proteins exhibit highly aggregation-sensitive structures. These proteins generally tend to aggregate and show higher yields of refolding in the presence of chaperones.
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© 2000 Humana Press Inc.
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Weber, F., Hayer-Hartl, M. (2000). Prevention of Rhodanese Aggregation by the Chaperonin GroEL. In: Schneider, C. (eds) Chaperonin Protocols. Methods in Molecular Biology, vol 140. Humana, Totowa, NJ. https://doi.org/10.1385/1-59259-061-6:111
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DOI: https://doi.org/10.1385/1-59259-061-6:111
Publisher Name: Humana, Totowa, NJ
Print ISBN: 978-0-89603-739-7
Online ISBN: 978-1-59259-061-2
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