Modeling the structure of helical assemblies with experimental constraints in Rosetta
(2018) In Methods in Molecular Biology 1764. p.475-489- Abstract
Determining high-resolution structures of proteins with helical symmetry can be challenging due to limitations in experimental data. In such instances, structure-based protein simulations driven by experimental data can provide a valuable approach for building models of helical assemblies. This chapter describes how the Rosetta macromolecular package can be used to model homomeric protein assemblies with helical symmetry in a range of modeling scenarios including energy refinement, symmetrical docking, comparative modeling, and de novo structure prediction. Data-guided structure modeling of helical assemblies with experimental information from electron density, X-ray fiber diffraction, solid-state NMR, and chemical cross-linking mass... (More)
Determining high-resolution structures of proteins with helical symmetry can be challenging due to limitations in experimental data. In such instances, structure-based protein simulations driven by experimental data can provide a valuable approach for building models of helical assemblies. This chapter describes how the Rosetta macromolecular package can be used to model homomeric protein assemblies with helical symmetry in a range of modeling scenarios including energy refinement, symmetrical docking, comparative modeling, and de novo structure prediction. Data-guided structure modeling of helical assemblies with experimental information from electron density, X-ray fiber diffraction, solid-state NMR, and chemical cross-linking mass spectrometry is also described.
(Less)
- author
- André, Ingemar LU
- organization
- publishing date
- 2018-01-01
- type
- Chapter in Book/Report/Conference proceeding
- publication status
- published
- subject
- keywords
- Fibers, Fibrils, Helical assemblies, Helical symmetry, Rosetta, Structure determination, Structure prediction
- host publication
- Methods in Molecular Biology
- series title
- Methods in Molecular Biology
- volume
- 1764
- pages
- 15 pages
- publisher
- Humana Press
- external identifiers
-
- scopus:85044834668
- pmid:29605934
- ISSN
- 1064-3745
- DOI
- 10.1007/978-1-4939-7759-8_30
- language
- English
- LU publication?
- yes
- id
- c59f9054-4c89-4d09-936d-5982c9d78f86
- date added to LUP
- 2018-04-16 14:07:48
- date last changed
- 2024-06-24 13:07:44
@inbook{c59f9054-4c89-4d09-936d-5982c9d78f86, abstract = {{<p>Determining high-resolution structures of proteins with helical symmetry can be challenging due to limitations in experimental data. In such instances, structure-based protein simulations driven by experimental data can provide a valuable approach for building models of helical assemblies. This chapter describes how the Rosetta macromolecular package can be used to model homomeric protein assemblies with helical symmetry in a range of modeling scenarios including energy refinement, symmetrical docking, comparative modeling, and de novo structure prediction. Data-guided structure modeling of helical assemblies with experimental information from electron density, X-ray fiber diffraction, solid-state NMR, and chemical cross-linking mass spectrometry is also described.</p>}}, author = {{André, Ingemar}}, booktitle = {{Methods in Molecular Biology}}, issn = {{1064-3745}}, keywords = {{Fibers; Fibrils; Helical assemblies; Helical symmetry; Rosetta; Structure determination; Structure prediction}}, language = {{eng}}, month = {{01}}, pages = {{475--489}}, publisher = {{Humana Press}}, series = {{Methods in Molecular Biology}}, title = {{Modeling the structure of helical assemblies with experimental constraints in Rosetta}}, url = {{http://dx.doi.org/10.1007/978-1-4939-7759-8_30}}, doi = {{10.1007/978-1-4939-7759-8_30}}, volume = {{1764}}, year = {{2018}}, }