Modeling the Tertiary Structure of the Rift Valley Fever Virus L Protein
| dc.contributor.author | Gogovi, Gideon K. | |
| dc.contributor.author | Almsned, Fahad | |
| dc.contributor.author | Bracci, Nicole | |
| dc.contributor.author | Kehn-Hall, Kylene | |
| dc.contributor.author | Shehu, Amarda | |
| dc.contributor.author | Blaisten-Barojas, Estela | |
| dc.date.accessioned | 2019-07-02T14:58:52Z | |
| dc.date.available | 2019-07-02T14:58:52Z | |
| dc.date.issued | 2019 | |
| dc.description.abstract | A tertiary structure governs, to a great extent, the biological activity of a protein in the living cell and is consequently a central focus of numerous studies aiming to shed light on cellular processes central to human health. Here, we aim to elucidate the structure of the Rift Valley fever virus (RVFV) L protein using a combination of in silico techniques. Due to its large size and multiple domains, elucidation of the tertiary structure of the L protein has so far challenged both dry and wet laboratories. In this work, we leverage complementary perspectives and tools from the computational-molecular-biology and bioinformatics domains for constructing, refining, and evaluating several atomistic structural models of the L protein that are physically realistic. All computed models have very flexible termini of about 200 amino acids each, and a high proportion of helical regions. Properties such as potential energy, radius of gyration, hydrodynamics radius, flexibility coefficient, and solvent-accessible surface are reported. Structural characterization of the L protein enables our laboratories to better understand viral replication and transcription via further studies of L protein-mediated protein–protein interactions. While results presented a focus on the RVFV L protein, the following workflow is a more general modeling protocol for discovering the tertiary structure of multidomain proteins consisting of thousands of amino acids. | |
| dc.identifier.doi | 10.3390/molecules24091768 | |
| dc.identifier.uri | https://hdl.handle.net/1920/11516 | |
| dc.language.iso | en_US | |
| dc.publisher | Molecules | |
| dc.rights | Attribution 3.0 United States | |
| dc.rights.uri | https://creativecommons.org/licenses/by/3.0/us/ | |
| dc.title | Modeling the Tertiary Structure of the Rift Valley Fever Virus L Protein | |
| dc.type | Article |