Zobrazeno 1 - 10
of 64
pro vyhledávání: '"Kate A. Stafford"'
Autor:
Fugate, Tally D.
Publikováno v:
Chronicles of Oklahoma; Summer2020, Vol. 98 Issue 2, p160-187, 28p
Publikováno v:
Journal of chemical information and modeling, vol 62, iss 5
Structure-based, virtual High-Throughput Screening (vHTS) methods for predicting ligand activity in drug discovery are important when there are no or relatively few known compounds that interact with a therapeutic target of interest. State-of-the-art
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::baaca5c81685cf7b70b816258cfbf346
https://pubmed.ncbi.nlm.nih.gov/35235748
https://pubmed.ncbi.nlm.nih.gov/35235748
Structure-based, virtual High Throughput Screening (vHTS) methods for predicting ligand activity in drug discovery are important when there are no or relatively few known compounds that interact with a therapeutic target of interest. State-of-the-art
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d393e429311af04f92fbc72de04f1f4
https://doi.org/10.26434/chemrxiv-2021-t6xkj
https://doi.org/10.26434/chemrxiv-2021-t6xkj
Autor:
Kate A. Stafford, Arthur G. Palmer III
Publikováno v:
F1000Research, Vol 3 (2014)
Ribonuclease H1 (RNase H) enzymes are well-conserved endonucleases that are present in all domains of life and are particularly important in the life cycle of retroviruses as domains within reverse transcriptase. Despite extensive study, especially o
Externí odkaz:
https://doaj.org/article/9bd53528e7df4ec8940eb889cbbf3681
Publikováno v:
PLoS Computational Biology, Vol 9, Iss 10, p e1003218 (2013)
The relationship between inherent internal conformational processes and enzymatic activity or thermodynamic stability of proteins has proven difficult to characterize. The study of homologous proteins with differing thermostabilities offers an especi
Externí odkaz:
https://doaj.org/article/aa71bc5fb4884397a514b1fd02b813a1
Publikováno v:
Journal of Chemical Theory and Computation. 12:2489-2492
Thermodynamic stability is a central requirement for protein function, and one goal of protein engineering is improvement of stability, particularly for applications in biotechnology. Herein, molecular dynamics simulations are used to predict in vitr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9472fc35247e67dd3fe551617e391fe5
https://doi.org/10.1021/acs.jctc.6b00120
https://doi.org/10.1021/acs.jctc.6b00120
Autor:
Arthur G. Palmer, Joel A. Butterwick, Richard A. Friesner, Robert Abel, Nikola Trbovic, Kate A. Stafford
Publikováno v:
Journal of Molecular Biology. 427:853-866
The conformational basis for reduced activity of the thermophilic ribonuclease HI enzyme from Thermus thermophilus, compared to its mesophilic homolog from Escherichia coli, is elucidated using a combination of NMR spectroscopy and molecular dynamics
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d35c94e10d1ad5fee7c9427ce438866
https://doi.org/10.1016/j.jmb.2014.11.023
https://doi.org/10.1016/j.jmb.2014.11.023
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 81:499-509
Factors affecting the accuracy of molecular dynamics (MD) simulations are investigated by comparing generalized order parameters for backbone NH vectors of the B3 immunoglobulin-binding domain of streptococcal protein G (GB3) derived from simulations
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::76eb2c92aab6b6f6326e3636108fa5a7
https://doi.org/10.1002/prot.24209
https://doi.org/10.1002/prot.24209
Publikováno v:
Journal of the American Chemical Society. 134:6365-6374
In this investigation, semiempirical NMR chemical shift prediction methods are used to evaluate the dynamically averaged values of backbone chemical shifts obtained from unbiased molecular dynamics (MD) simulations of proteins. MD-averaged chemical s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d7f1fef845e027b977c3916e346b41c
https://doi.org/10.1021/ja300265w
https://doi.org/10.1021/ja300265w
Autor:
Kate A. Stafford, Paul Maragakis, Justin Gullingsrud, Yibing Shan, Stefano Piana, Patrick J. Miller, Michael P. Eastwood, C. A. Rendleman, Willy Wriggers, Kresten Lindorff-Larsen, David E. Shaw, Ron O. Dror
Publikováno v:
Journal of Chemical Theory and Computation. 5:2595-2605
Events of scientific interest in molecular dynamics (MD) simulations, including conformational changes, folding transitions, and translocations of ligands and reaction products, often correspond to high-level structural rearrangements that alter cont
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32fd70d472ea5b058a6c689d746e37a9
https://doi.org/10.1021/ct900229u
https://doi.org/10.1021/ct900229u