Zobrazeno 1 - 10
of 192
pro vyhledávání: '"John T M, Kennis"'
Autor:
Matthias Broser, Anika Spreen, Patrick E. Konold, Enrico Schiewer, Suliman Adam, Veniamin Borin, Igor Schapiro, Reinhard Seifert, John T. M. Kennis, Yinth Andrea Bernal Sierra, Peter Hegemann
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-1 (2024)
Externí odkaz:
https://doaj.org/article/66437da637c848348ff049b21ce79cbc
Autor:
Arita Silapetere, Songhwan Hwang, Yusaku Hontani, Rodrigo G. Fernandez Lahore, Jens Balke, Francisco Velazquez Escobar, Martijn Tros, Patrick E. Konold, Rainer Matis, Roberta Croce, Peter J. Walla, Peter Hildebrandt, Ulrike Alexiev, John T. M. Kennis, Han Sun, Tillmann Utesch, Peter Hegemann
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-20 (2022)
The authors present an in-depth investigation of excited state dynamics and molecular mechanism of the voltage sensing in microbial rhodopsins. Using a combination of spectroscopic investigations and molecular dynamics simulations, the study proposes
Externí odkaz:
https://doaj.org/article/2a436882e40e4c79b7b00aa20fa1dce0
Autor:
Janneke Ravensbergen, Smitha Pillai, Dalvin D. Méndez-Hernández, Raoul N. Frese, Rienk van Grondelle, Devens Gust, Thomas A. Moore, Ana L. Moore, John T. M. Kennis
Publikováno v:
ACS Physical Chemistry Au, Vol 2, Iss 1, Pp 59-67 (2021)
Externí odkaz:
https://doaj.org/article/0ccf14cb894444cead412780cccedb39
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
Photosystem II subunit S (PsbS) senses thylakoid lumen acidification when plants are exposed to excess light. Here the authors use NMR and IR spectroscopy to show that low pH causes repositioning of an amphipathic helix and folding of a loop involvin
Externí odkaz:
https://doaj.org/article/7f3ec82616f347c08d46176fe6aab794
Autor:
Yusaku Hontani, Mikhail Baloban, Francisco Velazquez Escobar, Swetta A. Jansen, Daria M. Shcherbakova, Jörn Weißenborn, Miroslav Kloz, Maria Andrea Mroginski, Vladislav V. Verkhusha, John T. M. Kennis
Publikováno v:
Communications Chemistry, Vol 4, Iss 1, Pp 1-11 (2021)
Near-infrared fluorescent proteins engineered from bacterial phytochromes are important for deep-tissue imaging in vivo, but the mechanism through which they bind to chromophores is not fully understood. Here the authors structurally analyze biliverd
Externí odkaz:
https://doaj.org/article/27b7026a2cc7487aa17fc5c6ab44f7c5
Autor:
Matthias Broser, Anika Spreen, Patrick E. Konold, Enrico Schiewer, Suliman Adam, Veniamin Borin, Igor Schapiro, Reinhard Seifert, John T. M. Kennis, Yinth Andrea Bernal Sierra, Peter Hegemann
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
Abstract The Rhizoclosmatium globosum genome encodes three rhodopsin-guanylyl cyclases (RGCs), which are predicted to facilitate visual orientation of the fungal zoospores. Here, we show that RGC1 and RGC2 function as light-activated cyclases only up
Externí odkaz:
https://doaj.org/article/10eb544325fe4b8da25b941e9130ed31
Autor:
Patrick E. Konold, Enis Arik, Jörn Weißenborn, Jos C. Arents, Klaas J. Hellingwerf, Ivo H. M. van Stokkum, John T. M. Kennis, Marie Louise Groot
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
Protein structural dynamics can be studied by time-resolved crystallography (TRC) and ultrafast transient spectroscopic methods. Here, the authors perform electronic and vibrational transient absorption measurements to characterise the full photocycl
Externí odkaz:
https://doaj.org/article/2f846740cfbb4428b7a602dd2a81f7d1
Autor:
Arita Silapetere, Songhwan Hwang, Yusaku Hontani, Rodrigo G. Fernandez Lahore, Jens Balke, Francisco Velazquez Escobar, Martijn Tros, Patrick E. Konold, Rainer Matis, Roberta Croce, Peter J. Walla, Peter Hildebrandt, Ulrike Alexiev, John T. M. Kennis, Han Sun, Tillmann Utesch, Peter Hegemann
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-1 (2022)
Externí odkaz:
https://doaj.org/article/3c972fcfbf3e4d4c940fb564f00f741b
Publikováno v:
ACS Omega, Vol 4, Iss 1, Pp 1238-1243 (2019)
Externí odkaz:
https://doaj.org/article/0fbd8bc8c87f496fa9041f98545043ff
Autor:
Yusaku Hontani, Marco Marazzi, Katja Stehfest, Tilo Mathes, Ivo H. M. van Stokkum, Marcus Elstner, Peter Hegemann, John T. M. Kennis
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
Abstract Channelrhodopsin (ChR) is a key protein of the optogenetic toolkit. C1C2, a functional chimeric protein of Chlamydomonas reinhardtii ChR1 and ChR2, is the only ChR whose crystal structure has been solved, and thus uniquely suitable for struc
Externí odkaz:
https://doaj.org/article/55c88734e4454dd4b7fde387a502ba5e