SMOG 2 and OpenSMOG: Extending the limits of structure‐based models-Reference-Cited by-同舟云学术

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SMOG 2 and OpenSMOG: Extending the limits of structure‐based models

Published:2021-11 Issue:1 Volume:31 Page:158-172
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Oliveira Antonio B.¹^ORCID,Contessoto Vinícius G.¹^ORCID,Hassan Asem²³^ORCID,Byju Sandra²³,Wang Ailun³^ORCID,Wang Yang⁴,Dodero‐Rojas Esteban¹^ORCID,Mohanty Udayan⁴^ORCID,Noel Jeffrey K.⁵^ORCID,Onuchic Jose N.¹⁶⁷⁸^ORCID,Whitford Paul C.²³^ORCID

Affiliation:

1. Center for Theoretical Biological Physics Rice University Houston Texas USA

2. Department of Physics Northeastern University, Dana Research Center Boston Massachusetts USA

3. Center for Theoretical Biological Physics Northeastern University Boston Massachusetts USA

4. Department of Chemistry Boston College Chestnut Hill Massachusetts USA

5. Crystallography Max Delbrück Center for Molecular Medicine Berlin Germany

6. Department of Physics & Astronomy Rice University Houston Texas USA

7. Department of Chemistry Rice University Houston Texas USA

8. Department of Biosciences Rice University Houston Texas USA

Funder

National Science Foundation of Sri Lanka

Welch Foundation

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.4209

Reference52 articles.

1. The Many Faces of Structure-Based Potentials: From Protein Folding Landscapes to Structural Characterization of Complex Biomolecules

2. A Survey of Flexible Protein Binding Mechanisms and their Transition States Using Native Topology Based Energy Landscapes

3. Studying ribosome dynamics with simplified models

4. Protein-guided RNA dynamics during early ribosome assembly

5. Topological and energetic factors: what determines the structural details of the transition state ensemble and “en-route” intermediates for protein folding? an investigation for small globular proteins

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4. Accurate Characterization of Binding Kinetics and Allosteric Mechanisms for the HSP90 Chaperone Inhibitors Using AI-Augmented Integrative Biophysical Studies;JACS Au;2024-04-01

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