Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Myung Kook Son"'
Autor:
Meenal Kataria, Youngseo Kim, Hong Diem Chau, Na Yeon Kwon, Yongju Hong, Taekyung Kim, Jaewan Ko, Myung Kook Son, Joona Bang, Sungnam Park, Hugh I. Kim, Kwangyeol Lee, Dong Hoon Choi
Publikováno v:
Journal of Materials Chemistry C. 10:10679-10685
Solvent mediated thermodynamically supramolecular assemblies of derivative 4 in aqueous media and recognition behavior in the presence of achiral/chiral analytes.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7ecf8ca2328bebfc1e69ec0677ad56e5
https://doi.org/10.1039/d2tc01113a
https://doi.org/10.1039/d2tc01113a
Publikováno v:
Journal of the American Society for Mass Spectrometry. 32:2528-2535
Hemoglobin (Hb) is a major oxygen-transporting protein with allosteric properties reflected in the structural changes that accompany binding of O2. Glycated hemoglobin (GHb), which is a minor component of human red cell hemolysate, is generated by a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec427edb4d9af29772238a133b9ae482
https://doi.org/10.1021/jasms.1c00161
https://doi.org/10.1021/jasms.1c00161
Publikováno v:
Journal of the American Chemical Society. 144(4)
Several point mutations can modulate protein structure and dynamics, leading to different natures. Especially in the case of amyloidogenic proteins closely related to neurodegenerative diseases, structural changes originating from point mutations can
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a19671a5014b69a629e6cf24015e23db
https://pubmed.ncbi.nlm.nih.gov/35073692
https://pubmed.ncbi.nlm.nih.gov/35073692
Autor:
So Yeon Chun, Myung Kook Son, Chae Ri Park, Chaiho Lim, Hugh I. Kim, Kyungwon Kwak, Minhaeng Cho
Publikováno v:
Chemical science. 13(16)
This study aims to understand the structural transition dynamics of INS during amyloid aggregation in H2O using 2D-IR spectroscopy. The results show that distinct fibrillations in D2O and H2O originated from different quaternary structures of INS.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5120b5d750f4e7d83c8daacfc6b65eba
https://pubmed.ncbi.nlm.nih.gov/35656138
https://pubmed.ncbi.nlm.nih.gov/35656138
Publikováno v:
Mass Spectrometry Reviews. 38:483-500
Flexible structures of intrinsically disordered proteins (IDPs) are crucial for versatile functions in living organisms, which involve interaction with diverse partners. Electrospray ionization ion mobility mass spectrometry (ESI-IM-MS) has been wide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8d05175b0a8e14d355389a6a218cc48
https://doi.org/10.1002/mas.21596
https://doi.org/10.1002/mas.21596
Autor:
Chae Eun Heo1,2, Minji Kim1,2, Myung Kook Son1,2, Da Gyeong Hyun1,2, Sung Woo Heo3 sungwoo.heo@kriss.re.kr, Kim, Hugh I.1,2 hughkim@korea.ac.kr
Publikováno v:
Journal of the American Society for Mass Spectrometry. 10/6/2021, Vol. 32 Issue 10, p2528-2535. 8p.