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Ministry points: Help
| Year | Points | List |
|---|---|---|
| Year 2024 | 140 | Ministry scored journals list 2024 |
| Year | Points | List |
|---|---|---|
| 2024 | 140 | Ministry scored journals list 2024 |
| 2023 | 140 | Ministry Scored Journals List |
| 2022 | 140 | Ministry Scored Journals List 2019-2022 |
| 2021 | 140 | Ministry Scored Journals List 2019-2022 |
| 2020 | 140 | Ministry Scored Journals List 2019-2022 |
| 2019 | 140 | Ministry Scored Journals List 2019-2022 |
Model:
Points CiteScore:
| Year | Points |
|---|---|
| Year 2022 | 4.8 |
| Year | Points |
|---|---|
| 2022 | 4.8 |
| 2021 | 3.5 |
| 2020 | 4.1 |
| 2019 | 5.1 |
| 2018 | 5.4 |
| 2017 | 4.2 |
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Papers published in journal
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total: 3
Catalog Journals
Year 2022
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Improvements and new functionalities of UNRES server for coarse-grained modeling of protein structure, dynamics, and interactions
PublicationIn this paper we report the improvements and extensions of the UNRES server (https://unres-server.chem.ug.edu.pl) for physics-based simulations with the coarse-grained UNRES model of polypeptide chains. The improvements include the replacement of the old code with the recently optimized one and adding the recent scale-consistent variant of the UNRES force field, which performs better in the modeling of proteins with the β and the...
Year 2021
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Molecular Dynamics to Predict Cryo-EM: Capturing Transitions and Short-Lived Conformational States of Biomolecules
PublicationSingle-particle cryogenic electron microscopy (cryo-EM) has revolutionized the field of the structural biology, providing an access to the atomic resolution structures of large biomolecular complexes in their near-native environment. Today’s cryo-EM maps can frequently reach the atomic-level resolution, while often containing a range of resolutions, with conformationally variable regions obtained at 6 Å or worse. Low resolution...
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Recent Developments in Data-Assisted Modeling of Flexible Proteins
PublicationMany 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...
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