Integration of Nanometer-Range Label-to-Label Distances and Their Distributions into Modelling Approaches
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Abstract
Labelling techniques such as electron paramagnetic resonance spectroscopy and single-molecule fluorescence resonance energy transfer, allow access to distances in the range of tens of angstroms, corresponding to the size of proteins and small to medium-sized protein complexes. Such measurements do not require long-range ordering and are therefore applicable to systems with partial disorder. Data from spin-label-based measurements can be processed into distance distributions that provide information about the extent of such disorder. Using such information in modelling presents several challenges, including a small number of restraints, the influence of the label itself on the measured distance and distribution width, and balancing the fitting quality of the long-range restraints with the fitting quality of other restraint subsets. Starting with general considerations about integrative and hybrid structural modelling, this review provides an overview of recent approaches to these problems and identifies where further progress is needed.
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Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
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- Authors
- Jeschke, G.
- Affiliations
- ETH Zurich (CH)
- Corresponding author
- Jeschke, Gunnar
- ORCID
- Jeschke, Gunnar
- Venue
- Biomolecules
- Publisher
- MDPI AG
- Published
- 2022-09-25
- Volume
- 12
- Issue
- 10
- Pages
- 1369
- ISSN
- 2218-273X (ISSN-L)
- PMC
- PMC9599366
- OpenAlex
- W4297146368
- Cited by
- 13
- References
- 3
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 3 · 2023: 5 · 2022: 1
- FWCI
- 0.29
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Biomolecules (publishedVersion, cc-by)
- Preprints.org (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Repository for Publications and Research Data (ETH Zurich) (submittedVersion, cc-by)
- ETH Zürich Research Collection
- Funders
- Swiss National Science Foundation (200020_188467)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Electron Spin Resonance Studies
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- distance distribution, spin labels, electron spin resonance, single-molecule fluorescence resonance energy transfer, protein complexes, partial disorder, protein structure determination
- MeSH terms
- Electron Spin Resonance Spectroscopy, Models, Molecular, Proteins, Spin Labels
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