Zobrazeno 1 - 10
of 52
pro vyhledávání: '"Do Soo Jang"'
Autor:
Se Jin Im, Sang In Yang, Se Hwan Yang, Dong Hoon Choi, So Young Choi, Hea Sook Kim, Do Soo Jang, Kyeong Sik Jin, Yo-Kyung Chung, Seung-Hee Kim, Sang Hoon Paik, Yoo Chang Park, Moon Koo Chung, Yong Bum Kim, Kang-Hyun Han, Kwan Yong Choi, Young Chul Sung
Publikováno v:
PLoS ONE, Vol 6, Iss 9, p e24574 (2011)
Human IgG1 Fc has been widely used as a bioconjugate, but exhibits shortcomings, such as antibody- and complement-mediated cytotoxicity as well as decreased bioactivity, when applied to agonistic proteins. Here, we constructed a nonimmunogenic, noncy
Externí odkaz:
https://doaj.org/article/5a9c73e6d3dc46749be05e8572f27352
Autor:
Dongwoo Ko, Jae Chan Park, Min-Kyong Hyon, Young Hyun Park, Gil-Jung Kim, Jong Beom Ku, Iseul Eom, Su Bin Lee, Jeong Mi Yun, Dan Bee Park, Do Yeon Kim, HyeHyeon Jang, Sora Lim, Do Soo Jang, Sung Yoo Cho, Chun Pyo Hong, Myung Ho Jang
Publikováno v:
Regular and Young Investigator Award Abstracts.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a1f393614b918c23b8f742deb41d9317
https://doi.org/10.1136/jitc-2022-sitc2022.0349
https://doi.org/10.1136/jitc-2022-sitc2022.0349
Publikováno v:
Amino Acids. 49:715-723
We analyzed the structure of horseradish peroxidase (HRP) under denaturing conditions of 9 M urea or 6 M guanidine hydrochloride (GdnHCl). Far-UV circular dichroism (CD) spectra indicated the existence of native-like secondary structure of holo-HRP i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f00e8d99a8f4d3073e0a681ef76d23d
https://doi.org/10.1007/s00726-016-2372-3
https://doi.org/10.1007/s00726-016-2372-3
Autor:
Bee Hak Hong, Kwan Yong Choi, Hyung Jin Cha, Jehan Kim, Kyeong Sik Jin, Hee Cheon Lee, Hyeong Ju Lee, Moonhor Ree, Do Soo Jang, Eung-Sam Kim
Publikováno v:
Science of Advanced Materials. 6:2325-2333
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dd93062cbf3eee92fb75881f4bcd6ce2
https://doi.org/10.1166/sam.2014.2202
https://doi.org/10.1166/sam.2014.2202
Autor:
Hyeong Ju Lee1, Do Soo Jang2, Hyung Jin Cha3, Hye Seon Moon1, Bee Hak Hong3, Kwan Yong Choi3 kchoi@postech.ac.kr, Hee Cheon Lee1 hcl@postech.ac.kr
Publikováno v:
Journal of Biochemistry. Aug2008, Vol. 144 Issue 2, p215-221. 7p.
Autor:
Bee Hak Hong, Kwan Yong Choi, Hyung Jin Cha, Jae Sung Woo, Do Soo Jang, Yeon Gil Kim, Kyong-Tai Kim
Publikováno v:
Molecules and Cells. 36:39-46
Proteins have evolved to compensate for detrimental mutations. However, compensatory mechanisms for protein defects are not well understood. Using ketosteroid isomerase (KSI), we investigated how second-site mutations could recover defective mutant f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ff3f4707cb706ef58935a94226ae214
https://doi.org/10.1007/s10059-013-0013-1
https://doi.org/10.1007/s10059-013-0013-1
Autor:
Bee Hak Hong, Kwan Yong Choi, Hyung Jin Cha, Jae-Hee Jeong, Eun Ju Shin, Young Sung Yun, Do Soo Jang
Publikováno v:
Biochimica et biophysica acta. 1864(10)
Ketosteroid isomerase (3-oxosteroid Δ(5)-Δ(4)-isomerase, KSI) from Pseudomonas putida catalyzes allylic rearrangement of the 5,6-double bond of Δ(5)-3-ketosteroid to 4,5-position by stereospecific intramolecular transfer of a proton. The active si
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7f8dfe50ea6ceac037dcdbc3f65cf91
https://pubmed.ncbi.nlm.nih.gov/27375051
https://pubmed.ncbi.nlm.nih.gov/27375051
Publikováno v:
Journal of Biological Chemistry. 277:23414-23419
In the equilibrium unfolding process of Δ5-3-ketosteroid isomerase from Pseudomonas testosteroni by urea, it was observed that the enzyme stability increases by 2.5 kcal/mol in the presence of 5% trifluoroethanol (TFE). To elucidate the increased en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b2e823e38640e59932a53e745bce251f
https://doi.org/10.1074/jbc.m200147200
https://doi.org/10.1074/jbc.m200147200
Contribution of a low-barrier hydrogen bond to catalysis is not significant in ketosteroid isomerase
Autor:
Bee Hak Hong, Kwan Yong Choi, Hyung Jin Cha, Sejeong Shin, Do Soo Jang, Gildon Choi, Hyeong Ju Lee, Hee Cheon Lee
Publikováno v:
Molecules and Cells
Low-barrier hydrogen bonds (LBHBs) have been proposed to have important influences on the enormous reaction rate increases achieved by many enzymes. Δ(5)-3-ketosteroid isomerase (KSI) catalyzes the allylic isomerization of Δ(5)-3-ketosteroid to its
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6c697a4407069e4c44ce2dcb8cd54df
https://pubmed.ncbi.nlm.nih.gov/25947291
https://pubmed.ncbi.nlm.nih.gov/25947291
Publikováno v:
Biochemistry. 40:5011-5017
Ketosteroid isomerase (KSI) from Comamonas testosteroni is a homodimeric enzyme with 125 amino acids in each monomer catalyzing the allylic isomerization reaction at rates comparable to the diffusion limit. Kinetic analysis of KSI refolding has been
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd837155f38ba8b3c6976fc675ebc621
https://doi.org/10.1021/bi0019139
https://doi.org/10.1021/bi0019139