Zobrazeno 1 - 10
of 109
pro vyhledávání: '"Hoi Sung, Chung"'
Autor:
Krishna C. Suddala, Janghyun Yoo, Lixin Fan, Xiaobing Zuo, Yun-Xing Wang, Hoi Sung Chung, Jinwei Zhang
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-16 (2023)
Abstract T-box riboswitches are multi-domain noncoding RNAs that surveil individual amino acid availabilities in most Gram-positive bacteria. T-boxes directly bind specific tRNAs, query their aminoacylation status to detect starvation, and feedback c
Externí odkaz:
https://doaj.org/article/66d1d3cbe7b549c88a45da47f25295bd
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
Three-colour FRET is a powerful tool to study macromolecular conformational dynamics, but is temporally limited due to the experimental complexity. Here the authors develop experimental and analytical methods for probing submillisecond-time scale dyn
Externí odkaz:
https://doaj.org/article/43303b5b95fe4c4c8636c35d24a12b28
Autor:
Eitan Lerner, Anders Barth, Jelle Hendrix, Benjamin Ambrose, Victoria Birkedal, Scott C Blanchard, Richard Börner, Hoi Sung Chung, Thorben Cordes, Timothy D Craggs, Ashok A Deniz, Jiajie Diao, Jingyi Fei, Ruben L Gonzalez, Irina V Gopich, Taekjip Ha, Christian A Hanke, Gilad Haran, Nikos S Hatzakis, Sungchul Hohng, Seok-Cheol Hong, Thorsten Hugel, Antonino Ingargiola, Chirlmin Joo, Achillefs N Kapanidis, Harold D Kim, Ted Laurence, Nam Ki Lee, Tae-Hee Lee, Edward A Lemke, Emmanuel Margeat, Jens Michaelis, Xavier Michalet, Sua Myong, Daniel Nettels, Thomas-Otavio Peulen, Evelyn Ploetz, Yair Razvag, Nicole C Robb, Benjamin Schuler, Hamid Soleimaninejad, Chun Tang, Reza Vafabakhsh, Don C Lamb, Claus AM Seidel, Shimon Weiss
Publikováno v:
eLife, Vol 10 (2021)
Single-molecule FRET (smFRET) has become a mainstream technique for studying biomolecular structural dynamics. The rapid and wide adoption of smFRET experiments by an ever-increasing number of groups has generated significant progress in sample prepa
Externí odkaz:
https://doaj.org/article/acccb8f6f1f1430c8cef78416466d619
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
Intrinsically disordered proteins (IDPs) usually fold during binding to target proteins which involves the formation of a transient complex (TC). Here authors use single-molecule FRET to show that the lifetime of TC for IDP binding is very long due t
Externí odkaz:
https://doaj.org/article/70516a3454314676950dba1a16adcf2d
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
Nature Communications
Nature Communications
We describe theory, experiments, and analyses of three-color Förster resonance energy transfer (FRET) spectroscopy for probing sub-millisecond conformational dynamics of protein folding and binding of disordered proteins. We devise a scheme that use
Publikováno v:
Proceedings of the National Academy of Sciences. 119
Polymorphism in the structure of amyloid fibrils suggests the existence of many different assembly pathways. Characterization of this heterogeneity is the key to understanding the aggregation mechanism and toxicity, but in practice it is extremely di
Publikováno v:
Biophysical Journal. 122:9a
Autor:
Hoi Sung Chung, Irina V. Gopich
Publikováno v:
Protein Folding ISBN: 9781071617151
Inter-dye distances and conformational dynamics can be studied using single-molecule FRET measurements. We consider two approaches to analyze sequences of photons with recorded photon colors and arrival times. The first approach is based on FRET effi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::89937c87f868b706cdf34b66ab6ff798
https://doi.org/10.1007/978-1-0716-1716-8_14
https://doi.org/10.1007/978-1-0716-1716-8_14
Autor:
Irina V, Gopich, Hoi Sung, Chung
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2376
Inter-dye distances and conformational dynamics can be studied using single-molecule FRET measurements. We consider two approaches to analyze sequences of photons with recorded photon colors and arrival times. The first approach is based on FRET effi
Autor:
Yusuke Okuno, Robert B. Best, Janghyun Yoo, G. Marius Clore, Charles D. Schwieters, Hoi Sung Chung
Publikováno v:
Proc Natl Acad Sci U S A
The cosolvent effect arises from the interaction of cosolute molecules with a protein and alters the equilibrium between native and unfolded states. Denaturants shift the equilibrium toward the latter, while osmolytes stabilize the former. The molecu