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Abstract
Many proteins can fold into well-defined conformations. However, intrinsically-disordered proteins (IDPs) do not possess a defined structure. Moreover, folded multi-domain proteins often digress into alternative conformations. Collectively, the conformational dynamics enables these proteins to fulfill specific functions. Thus, most experimental observables are averaged over the conformations that constitute an ensemble. In this article, we review the recent developments in the concept and methods for the determination of the dynamic structures of flexible peptides and proteins. In particular, we describe ways to extract information from nuclear magnetic resonance small-angle X-ray scattering (SAXS), and chemical cross-linking coupled with mass spectroscopy (XL-MS) measurements. All these techniques can be used to obtain ensemble-averaged restraints or to re-weight the simulated conformational ensembles.
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Web of Science
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Authors (6)
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Cezary Czaplewski Dr hab.
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Zhou Gong
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Kai Xue
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Chun Tang
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Adam Liwo
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Full text
- Publication version
- Accepted or Published Version
- DOI:
- Digital Object Identifier (open in new tab) 10.3389/fmolb.2021.765562
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Details
- Category:
- Articles
- Type:
- artykuły w czasopismach
- Published in:
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Frontiers in Molecular Biosciences
no. 8,
ISSN: - Language:
- English
- Publication year:
- 2021
- Bibliographic description:
- Czaplewski C., Gong Z., Lubecka E., Xue K., Tang C., Liwo A.: Recent Developments in Data-Assisted Modeling of Flexible Proteins// Frontiers in Molecular Biosciences -Vol. 8, (2021), s.765562-
- DOI:
- Digital Object Identifier (open in new tab) 10.3389/fmolb.2021.765562
- Verified by:
- Gdańsk University of Technology
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