Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Geir Villy Isaksen"'
Autor:
Davide Michetti, Bjørn Olav Brandsdal, Davide Bon, Geir Villy Isaksen, Matteo Tiberti, Elena Papaleo
Publikováno v:
PLoS ONE, Vol 12, Iss 2, p e0169586 (2017)
The psychrophilic and mesophilic endonucleases A (EndA) from Aliivibrio salmonicida (VsEndA) and Vibrio cholera (VcEndA) have been studied experimentally in terms of the biophysical properties related to thermal adaptation. The analyses of their stat
Externí odkaz:
https://doaj.org/article/23cd72f0154344eb86573bf533151c35
Publikováno v:
PLoS Computational Biology, Vol 10, Iss 8, p e1003813 (2014)
Life has effectively colonized most of our planet and extremophilic organisms require specialized enzymes to survive under harsh conditions. Cold-loving organisms (psychrophiles) express heat-labile enzymes that possess a high specific activity and c
Externí odkaz:
https://doaj.org/article/767f4a5cb980494391c2e76145da131c
Autor:
Ryan Scott Wilkins, Bjarte Aarmo Lund, Geir Villy Isaksen, Johan Åqvist, Bjørn Olav Brandsdal
Chorismate mutases have extensively been used as computational benchmarking systems for enzyme catalysis, yet the roles entropy and enthalpy play in catalysis are still not fully understood. Thus, it is important to better understand these enzymes fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::376419980093c27cf93a2949af25b8fa
https://doi.org/10.1101/2023.04.20.537678
https://doi.org/10.1101/2023.04.20.537678
Autor:
Geir Villy Isaksen, Maria Selmer, Jon Jerlström-Hultqvist, Xiaohu Guo, Adolf Gogoll, Silvia Trigüis, Omar Warsi, Ulrich Eckhard, Annika Söderholm, Sandesh Kanchugal P, Dan I. Andersson, Johan Åqvist
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::41e96188c6d425b9bcd4e05ff824a084
https://doi.org/10.7554/elife.61818.sa2
https://doi.org/10.7554/elife.61818.sa2
Autor:
Silvia Trigüis, Annika Söderholm, Ulrich Eckhard, Maria Selmer, Dan I. Andersson, Geir Villy Isaksen, Xiaohu Guo, Johan Åqvist, Sandesh Kanchugal P, Jon Jerlström-Hultqvist, Adolf Gogoll, Omar Warsi
The first SAM degrading enzyme (SAMase) was discovered in bacteriophage T3, as a counter-defense against the bacterial restriction-modification system, and annotated as an S-adenosyl-L-methionine (SAM) hydrolase forming 5’-methyl-thioadenosine (MTA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::188181231d07312eac9febbd2d5b00d6
https://doi.org/10.1101/2020.08.16.253161
https://doi.org/10.1101/2020.08.16.253161
Publikováno v:
Scientific Reports, Vol 9, Iss 1, Pp 1-10 (2019)
Scientific Reports
Scientific Reports
Cold-adapted enzymes from psychrophilic species achieve their high catalytic efficiency at low temperature by a different partitioning of the activation free energy into its enthalpic and entropic components, compared to orthologous mesophilic enzyme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5726101f3baafeefd6d95792f36ef79
https://hdl.handle.net/10037/17530
https://hdl.handle.net/10037/17530
Autor:
Hugo Gutiérrez-de-Terán, Silvana Vasile, Amber van Veen, Willem Jespers, Geir Villy Isaksen, Tor Arne Heim Andberg, Johan Åqvist, Bjørn Olav Brandsdal
Predicting the effect of single-point mutations on protein stability or protein−ligand binding is a major challenge in computational biology. Free energy calculations constitute the most rigorous approach to this problem, though the estimation of c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e99f00799bef3b576ee78808a21a7af
https://hdl.handle.net/10037/18010
https://hdl.handle.net/10037/18010
Publikováno v:
Proceedings of the National Academy of Sciences. 113:7822-7827
The structural origin of enzyme adaptation to low temperature, allowing efficient catalysis of chemical reactions even near the freezing point of water, remains a fundamental puzzle in biocatalysis. A remarkable universal fingerprint shared by all co
Publikováno v:
Biochemistry. 57(20)
The class I pancreatic elastase from Atlantic salmon is considered to be a cold-adapted enzyme in view of the cold habitat, the reduced thermostability of the enzyme, and the fact that it is faster than its mesophilic porcine counterpart at room temp
Publikováno v:
Journal of Molecular Graphics and Modelling. 60:15-23
Structural information and activity data has increased rapidly for many protein targets during the last decades. In this paper, we present a high-throughput interface (Qgui) for automated free energy and empirical valence bond (EVB) calculations that