Please use this identifier to cite or link to this item: 192.168.6.56/handle/123456789/74524
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dc.contributor.authorCohen, Sharona-
dc.date.accessioned2019-06-28T06:12:58Z-
dc.date.available2019-06-28T06:12:58Z-
dc.date.issued2016-
dc.identifier.isbn978-3-319-09558-5-
dc.identifier.urihttp://10.6.20.12:80/handle/123456789/74524-
dc.descriptionThe protein folding field has undergone enormous transformation in recent years, led mainly by the introduction of new techniques that facilitate the study of folding on the single-molecule level, based on either sensitive fluorescence methodology or force spectroscopy. The progress in the field has also been driven by the realization that, in addition to the more familiar globular proteins, there are novel groups of proteins whose folding behavior requires the development of new paradigms. Among these proteins are two important groups. The first is the group of intrinsically unfolded proteins, many of which fold only upon interaction with their binding partners. The second group includes the repeat proteins, a diverse set of proteins made of short structural units that repeat themselves and form nonglobular, elongated structures resembling solenoids.en
dc.languageenen
dc.language.isoenen_US
dc.publisherSpringer International Publishing Switzerlanden_US
dc.subjectChemistryen_US
dc.titleSingle-Molecule Fluorescence Spectroscopy of the Folding of a Repeat Proteinen_US
dc.typeBooken_US
Appears in Collections:Chemistry

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