Author

G. V. T. Swapna

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Biophysics· 2 Microbiology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Assay:protein structure· 3 Approach:statistical model· 3 Research Focus:chromatin & epigenetic regulation· 1 Approach:deep learning· 1 Approach:experimental assay· 1 Research Focus:host-pathogen & immune response· 1 Organism:mouse· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

G. T. Montelione· 3 shared J. Hao· 2 shared M. J. Roth· 2 shared A. Mondal· 1 shared A. Perez· 1 shared B. Jacobs· 1 shared C. A. Royer· 1 shared D. R. Colman· 1 shared

Activity by Year

2020-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersBiophysics

G. T. Montelione

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

BiophysicsbioRxivPreprintDec 31, 2021

Structure determination of protein-peptide complexes from NMR chemical shift data using MELD.

A. Mondal, G. V. T. Swapna, J. Hao…·A. Perez

The paper develops a hybrid MELD-NMR approach to determine structures of flexible protein-polypeptide complexes using only NMR chemical shift data, achieving accurate results for ET domain-BET protein interactions.

DOI 10.1101/2021.12.31.474671

protein structuredeep learning

𝕏 PostBluesky

BiophysicsbioRxivDec 28, 2021

Structural Evolution of the Ancient Enzyme, Dissimilatory Sulfite Reductase

D. R. Colman, G. Labesse, G. V. T. Swapna…·C. A. Royer

The paper investigates structural evolution of DsrAB across sulfate-reducing organisms, identifying conserved features and allostery-related co-variance patterns.

DOI 10.1002/prot.26315

protein structurestatistical model

𝕏 PostBluesky

MicrobiologybioRxivSep 21, 2020

A common binding motif in the ET domain of BRD3 forms polymorphic structural interfaces with host and viral proteins

S. Aiyer, G. V. T. Swapna, G. Liu…·M. J. Roth

This paper investigates the structural interactions of the BRD3 ET domain with host and viral proteins, revealing polymorphic structural interfaces and conformational plasticity.

DOI 10.1016/j.str.2021.01.010

mouseprotein structure

𝕏 PostBluesky