Zobrazeno 1 - 10
of 56
pro vyhledávání: '"Chiwook Park"'
Autor:
Chiwook Park
Publikováno v:
ACS Omega, Vol 9, Iss 44, Pp 44233-44240 (2024)
Externí odkaz:
https://doaj.org/article/8f4801b3fac141a69885e7ea620a494a
Publikováno v:
PLoS ONE, Vol 9, Iss 10, p e111416 (2014)
The proteolysis kinetics of intact proteins by nonspecific proteases provides valuable information on transient partial unfolding of proteins under native conditions. Native-state proteolysis is an approach to utilize the proteolysis kinetics to asse
Externí odkaz:
https://doaj.org/article/49454a8efec14b8a84e476a069a741fb
Autor:
Chiwook Park, Chen Chen
Publikováno v:
Protein Sci
Previously, we have reported that ATP accelerates the folding and unfolding of Escherichia coli glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH), which is a glycolytic enzyme utilizing NAD(+) as a cofactor. Because ATP and NAD(+) share the ADP mo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbd99890f71320ad5da8da8729f9687c
https://doi.org/10.1002/pro.3880
https://doi.org/10.1002/pro.3880
Autor:
Chiwook Park
The chemical kinetics is such a fundamental topic in chemistry. By analyzing how the experimental conditions and parameters influence the reaction rate, chemists have deciphered the molecular details on how the chemical reactions occur. The quantitat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::49342da0b686f9c3d77fc5ec7cb16d2f
https://doi.org/10.1101/2022.02.01.478700
https://doi.org/10.1101/2022.02.01.478700
Autor:
Chiwook Park
kcat and kcat/KM are the two fundamental kinetic parameters in enzyme kinetics. kcat is the first-order rate constant that determines the reaction rate when the enzyme is fully occupied at a saturating concentration of the substrate. kcat/KM is the s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ce28de9b8d698a82066faf532a169c3
https://doi.org/10.1101/2021.12.09.471995
https://doi.org/10.1101/2021.12.09.471995
Publikováno v:
Biochemistry. 56:6555-6564
Previously, we demonstrated that binding of a ligand to Escherichia coli cofactor-dependent phosphoglycerate mutase (dPGM), a homodimeric protein, is energetically coupled with dimerization. The equilibrium unfolding of dPGM occurs with a stable, mon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d479b81287ff97b8e8ef244641da79d7
https://doi.org/10.1021/acs.biochem.7b00850
https://doi.org/10.1021/acs.biochem.7b00850
Publikováno v:
NUCLEIC ACIDS RESEARCH(45): W1
Nucleic Acids Research
Nucleic Acids Research
Homo-oligomerization of proteins is abundant in nature, and is often intimately related with the physiological functions of proteins, such as in metabolism, signal transduction or immunity. Information on the homo-oligomer structure is therefore impo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2644d22f7b5224db87aec460cc8573af
https://doi.org/10.1093/nar/gkx246
https://doi.org/10.1093/nar/gkx246
Publikováno v:
Protein Science. 25:999-1009
Salt bridges are frequently observed in protein structures. Because the energetic contribution of salt bridges is strongly dependent on the environmental context, salt bridges are believed to contribute to the structural specificity rather than the s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::211b7c49eeadc04226ecfcbd38388a75
https://doi.org/10.1002/pro.2908
https://doi.org/10.1002/pro.2908
Autor:
Joseph R. Kasper, Chiwook Park
Publikováno v:
Protein Science. 24:129-137
The conformational energy landscape of a protein determines populations of all possible conformations of the protein and also determines the kinetics of the conversion between the conformations. Interaction with ligands influences the conformational
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::04911cb4e8c4bda3cf8cf8627f0770dd
https://doi.org/10.1002/pro.2596
https://doi.org/10.1002/pro.2596
Autor:
Daisuke Kihara, Lingfei Zeng, Woong-Hee Shin, Xiaolei Zhu, W. Andy Tao, Chiwook Park, Sung Hoon Park
Publikováno v:
Journal of proteome research. 16(2)
Protein–ligand interaction plays a critical role in regulating the biochemical functions of proteins. Discovering protein targets for ligands is vital to new drug development. Here, we present a strategy that combines experimental and computational
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61aeee4f902cef7df5fde889b0f7e7a4
https://pubmed.ncbi.nlm.nih.gov/28152599
https://pubmed.ncbi.nlm.nih.gov/28152599