Journal of biomolecular structure & dynamics.
Publisher:
Adenine Press,. Oxon, UK : Taylor & Francis (2012)
Frequency: Eighteen issues a year, 2019-
Country: England
Language: English
Start Year:1983 -
ISSN:
0739-1102 (Print)
1538-0254 (Electronic)
0739-1102 (Linking)
1538-0254 (Electronic)
0739-1102 (Linking)
Impact Factor
4.4
2022
| NLM ID: | 8404176 |
| (DNLM): | J14645000(s) |
| (OCoLC): | 09688706 |
| Coden: | JBSDD6 |
| LCCN: | 84640420 |
| Classification: | W1 JO564W |
Development of homology model, docking protocol and Machine-Learning based scoring functions for identification of Equus caballus’s butyrylcholinesterase inhibitors. Machine learning (ML), an emerging field in drug design, has the potential to predict toxicity, shape-based analysis of inhibitors, scoring function (SF) etc. In the present study, a homology model, docking protocol, and a dedicated SF have been developed to identify the inhibitors of horse butyrylcholinesterase (BChE) enzyme. Horse BChE enzyme has homology with human BChE and is a substitute for the screening of inhibitors. The developed homology model was validated and the active site residues were identified from Cavityplus to generate grid box for docking. The validation of docking invol...
The structural stability of wild-type horse prion protein. Prion diseases (e.g. Creutzfeldt-Jakob disease (CJD), variant CJD (vCJD), Gerstmann-Straussler-Scheinker syndrome (GSS), Fatal Familial Insomnia (FFI) and Kuru in humans, scrapie in sheep, bovine spongiform encephalopathy (BSE or 'mad-cow' disease) and chronic wasting disease (CWD) in cattles) are invariably fatal and highly infectious neurodegenerative diseases affecting humans and animals. However, by now there have not been some effective therapeutic approaches or medications to treat all these prion diseases. Rabbits, dogs, and horses are the only mammalian species reported to be resistant...
Molecular dynamics simulation of equine infectious anemia virus Tat protein in water and in 40% trifluoroethanol. Two molecular dynamics (MD) simulations were performed in order to increase the understanding of the dependence of protein conformation on solvent environment. The protein used for these simulations is the transcriptional activator of the equine infectious anemia virus (EIAV-Tat). The structure of this protein has been determined by nuclear magnetic resonance (NMR) in aqueous solution (Willbold et al., Science 264, 1584 (1994)) and in 40% (v/v) trifluoroethanol (TFE) (Sticht et al., Eur. J. Biochem., submitted) showing considerable differences in the stability of the secondary structure elemen...