Table 1.
Applications | Methodology used | Total Time | References |
---|---|---|---|
Αβ1-40, Αβ1-42, | HT-REMD | 70.0 μs | 167 |
WT(D23N) monomers and dimers | 97.5 μs | 168 | |
Trimers of Αβ17-42 and interactions with drugs | REMD | 16.4 μs | 96 |
Aggregation of 3- to 20-mers of amyloid fragments | MD ART REMD |
30.0 μs no 120.0 μs |
149, 150, 152 80,150 23, 68, 99, 149-153 |
Size of the primary nucleus for fibril formation | MD REMD |
33.8 μs 90.0 μs |
158 99, 153 |
Peptide Structure Prediction and Conformations of protein fragments | PEP-FOLD | no | 177, 178, 180, 182-189 |
Protein-peptide interactions | PEP-FOLD | no | 190-194 |
Design of immunogenic and antiviral peptides | PEP-FOLD | no | 195-201 |
Impact of macromolecules and hydrodynamics | MUPHY/OPEP | no | this work |
RNA and DNA folding | MD, REMD, ST | 85.0 μs | 231, 233, this work |
Thermophilic and mesophilic proteins | REMD | 72.0 μs | this work |
Impact of shear flow | MUPHY/OPEP | 30 ns | this work |
Virtual reality | Interactive MD | 0.2 ns | this work |