Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Tayler D. Hill"'
Protein motion is central to enzymatic catalysis but the influence of femtosecond – picosecond timescale fluctuations on chemical reaction steps remains poorly understood. One barrier to uniting experiment and theory is difficulty in resolving the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::68b9de84a15c4d9516a759080d74b57e
https://doi.org/10.26434/chemrxiv-2022-1r1b8
https://doi.org/10.26434/chemrxiv-2022-1r1b8
Publikováno v:
Biophysical Journal. 121:53a-54a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f97bf2c347bac875799418e54f7d4c78
https://doi.org/10.1016/j.bpj.2021.11.2466
https://doi.org/10.1016/j.bpj.2021.11.2466
Guanine-rich nucleic acid sequences have a tendency to form four-stranded non-canonical motifs known as G-quadruplexes. These motifs may adopt a wide range of structures characterized by size, strand orientation, guanine base conformation, and fold t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6b747736b414d1e2d9143437a5b4945
https://doi.org/10.1101/2021.07.13.452271
https://doi.org/10.1101/2021.07.13.452271
Publikováno v:
Protein Sci
Mitochondrial outer membrane permeabilization, which is a critical step in apoptosis, is initiated upon transmembrane insertion of the C-terminal α-helix (α9) of the proapoptotic Bcl-2 family protein BAX. The isolated α9 fragment (residues 173-192
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::375a33a33f64c4f4a21b8fafa0956ba1
https://pubmed.ncbi.nlm.nih.gov/33641228
https://pubmed.ncbi.nlm.nih.gov/33641228
Mitochondrial outer membrane permeabilization, which is a critical step in apoptosis, is initiated upon transmembrane insertion of the C-terminal α-helix (α9) of the pro-apoptotic Bcl-2 family protein BAX. The isolated α9 fragment (residues 173-19
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7734d4de60bf3bfa200c7c4638936aac
https://doi.org/10.1101/2020.10.20.347567
https://doi.org/10.1101/2020.10.20.347567
Publikováno v:
Biophysical Journal. 112:67a
Our research aims to understand how changes in ultrafast dynamics compare and correlate to thermophilic enzyme activity. We observe fluctuating electric field effects in a promiscuous, hyperthermophilic ene-reductase from Pyrococcus horikoshii (PhENR
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4f47a84b0aa8cae35f195555c6f51fa5
https://doi.org/10.1016/j.bpj.2016.11.400
https://doi.org/10.1016/j.bpj.2016.11.400