Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Kanokporn Chattrakun"'
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-9 (2017)
Abstract The electronic band structure of twisted bilayer graphene develops van Hove singularities whose energy depends on the twist angle between the two layers. Using Raman spectroscopy, we monitor the evolution of the electronic band structure upo
Externí odkaz:
https://doaj.org/article/c90559c9f6f3462ab60206ae436f8061
Publikováno v:
Langmuir. 35:12246-12256
Surface-supported lipid bilayers are used widely throughout the nanoscience community as cellular membrane mimics. For example, they are frequently employed in single-molecule atomic force microscopy (AFM) studies to shed light on membrane protein co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11207b20c4b5e25126100cdf4f2f49d1
https://doi.org/10.1021/acs.langmuir.9b01928
https://doi.org/10.1021/acs.langmuir.9b01928
Autor:
Kanokporn, Chattrakun, Katherine G, Schaefer, Lucas S, Chandler, Brendan P, Marsh, Gavin M, King
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2302
Atomic force microscopy has emerged as a valuable complementary technique in membrane structural biology. The apparatus is capable of probing individual membrane proteins in fluid lipid bilayers at room temperature with spatial resolution at the mole
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::529106387aeac8b585fd86762b5e938f
https://pubmed.ncbi.nlm.nih.gov/33877624
https://pubmed.ncbi.nlm.nih.gov/33877624
Autor:
Kanokporn Chattrakun, Brendan P. Marsh, Katherine G. Schaefer, Lucas S. Chandler, Gavin M. King
Publikováno v:
Methods in Molecular Biology ISBN: 9781071613931
Atomic force microscopy has emerged as a valuable complementary technique in membrane structural biology. The apparatus is capable of probing individual membrane proteins in fluid lipid bilayers at room temperature with spatial resolution at the mole
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3bc316f9d43fb0aaed020661c386147b
https://doi.org/10.1007/978-1-0716-1394-8_6
https://doi.org/10.1007/978-1-0716-1394-8_6
Autor:
Linda L. Randall, Raghavendar Reddy Sanganna Gari, Nagaraju Chada, Chunfeng Mao, Brendan P. Marsh, Kanokporn Chattrakun, Gavin M. King
Publikováno v:
Science Advances. 5
Escherichia coli exports proteins via a translocase comprising SecA and the translocon, SecYEG. Structural changes of active translocases underlie general secretory system function, yet directly visualizing dynamics has been challenging. We imaged ac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b37624dc6514557739c154a2e092596a
https://doi.org/10.1126/sciadv.aav9404
https://doi.org/10.1126/sciadv.aav9404
Publikováno v:
Langmuir. 36:6323-6323
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1769a14f157a4e85dd335e829677d1f
https://doi.org/10.1021/acs.langmuir.0c01279
https://doi.org/10.1021/acs.langmuir.0c01279
Publikováno v:
Biophysical Journal. 118:56a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7e2b7afd83f2516795651d232751f527
https://doi.org/10.1016/j.bpj.2019.11.484
https://doi.org/10.1016/j.bpj.2019.11.484
Autor:
Raghavendar Reddy, Sanganna Gari, Kanokporn, Chattrakun, Brendan P, Marsh, Chunfeng, Mao, Nagaraju, Chada, Linda L, Randall, Gavin M, King
Publikováno v:
Science Advances
We reveal the dynamic topography of active translocases as a function of precursor, nucleotide, and stage of translocation.
Escherichia coli exports proteins via a translocase comprising SecA and the translocon, SecYEG. Structural changes of act
Escherichia coli exports proteins via a translocase comprising SecA and the translocon, SecYEG. Structural changes of act
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::163fba09d52546651b7878e279c3c067
https://pubmed.ncbi.nlm.nih.gov/31206019
https://pubmed.ncbi.nlm.nih.gov/31206019
Publikováno v:
Biophysical Journal. 114:273a-274a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cd4714dd3e253386a3aa72bcbe2e81ba
https://doi.org/10.1016/j.bpj.2017.11.1580
https://doi.org/10.1016/j.bpj.2017.11.1580
Publikováno v:
Biophysical Journal. 116:300a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ec7c9ffdc0a471deeb37bd6227719f3b
https://doi.org/10.1016/j.bpj.2018.11.1625
https://doi.org/10.1016/j.bpj.2018.11.1625