Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Yun‐Hsuan Kuo"'
Autor:
Yun-Hsuan Kuo, Yun-Wei Chiang
Publikováno v:
ACS Central Science, Vol 4, Iss 5, Pp 645-655 (2018)
Externí odkaz:
https://doaj.org/article/7cc42e87195144ebb2e034ec7ed18cf5
Autor:
Yun-Hsuan Kuo, 郭芸瑄
101
The 2010 United States House of Representatives elections, Republicans gained control of the chamber, picking up a net total of 63 seats and erasing the gains Democrats made in 2006 and 2008. We also saw the rise of the Tea Party movement us
The 2010 United States House of Representatives elections, Republicans gained control of the chamber, picking up a net total of 63 seats and erasing the gains Democrats made in 2006 and 2008. We also saw the rise of the Tea Party movement us
Externí odkaz:
http://ndltd.ncl.edu.tw/handle/25593974117249093389
Autor:
Brett K.‐Y. Chu, Ruei‐Fong Tsai, Chien‐Lun Hung, Yun‐Hsuan Kuo, Eric H.‐L. Chen, Yun‐Wei Chiang, Sunney I. Chan, Rita P.‐Y. Chen
Publikováno v:
Protein Sci
Prion diseases are transmissible fatal neurodegenerative disorders spreading between humans and other mammals. The pathogenic agent, prion, is a protease‐resistant, β‐sheet‐rich protein aggregate, converted from a membrane protein called PrP(C
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44d40b2ca4f70cbaefdebc55f919edc4
https://europepmc.org/articles/PMC9112485/
https://europepmc.org/articles/PMC9112485/
Autor:
Yun-Wei Chiang, Yun-Hsuan Kuo, Te-Yu Kao, Nien-Chen Lin, Feng-Chun Lo, Ruei-Fong Tsai, Wen-Feng Liaw
Publikováno v:
The Journal of Physical Chemistry Letters. 11:8538-8542
The YtfE protein catalyzes the reduction of NO to N2O, protecting iron-sulfur clusters from nitrosylation. The structure of YtfE has a two-domain architecture, with a diiron-containing C-terminal domain linked to an N-terminal domain, in which the fu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a46839859e226512a542403f27f4190
https://doi.org/10.1021/acs.jpclett.0c02200
https://doi.org/10.1021/acs.jpclett.0c02200
Publikováno v:
The journal of physical chemistry. B. 125(30)
Understanding how proteins retain structural stability is not only of fundamental importance in biophysics but also critical to industrial production of antibodies and vaccines. Protein stability is known to depend mainly on two effects: internal hyd
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0904f7f97e74a9b0afbfbdccda41fcf2
https://pubmed.ncbi.nlm.nih.gov/34314184
https://pubmed.ncbi.nlm.nih.gov/34314184
Publikováno v:
Chemistry – An Asian Journal. 14:3981-3991
Spin-label electron spin resonance (ESR) has emerged as a powerful tool to characterize protein dynamics. One recent advance is the development of ESR for resolving dynamical components that occur or coexist during a biological process. It has been a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::301524ab7ef2f4b43b2bf6497bff3956
https://doi.org/10.1002/asia.201900855
https://doi.org/10.1002/asia.201900855
Publikováno v:
The journal of physical chemistry. B. 121(17)
The electron spin resonance (ESR) spectra of spin-labeled proteins are sensitive to dynamics, but discrimination between the various dynamics is often difficult. Here, we report an improvement in ESR spectral sensitivity to local backbone dynamics of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8b8cd58255ba23d6fd9acc7740c3a84
https://pubmed.ncbi.nlm.nih.gov/28409932
https://pubmed.ncbi.nlm.nih.gov/28409932
Publikováno v:
Langmuir. 29:13865-13872
Under nanoconfinement the formation of crystalline ice is suppressed, allowing the study of water dynamics at subfreezing temperatures. Here we report a temperature-dependent investigation (170-260 K) of the behavior of hydration water under nanoconf
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c4e7d990e125bf5a82877833f84f8b0
https://doi.org/10.1021/la403002t
https://doi.org/10.1021/la403002t
Autor:
Chung-Yu Lee, Rita P.-Y. Chen, Yun-Hsuan Kuo, Che Yang, Wei-Lin Lo, Yun-Wei Chiang, Jason C. Sang
Publikováno v:
ACS chemical biology. 10(2)
Under nondenaturing neutral pH conditions, full-length mouse recombinant prion protein lacking the only disulfide bridge can spontaneously convert from an α-helical-dominant conformer (α-state) to a β-sheet-rich conformer (β-state), which then as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd7afd6753aee4dd8ec6da4b5051d381
https://pubmed.ncbi.nlm.nih.gov/25375095
https://pubmed.ncbi.nlm.nih.gov/25375095