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Shiraga, Keiichiro, Urabe, Mako, Matsui, Takeshi, Kikuchi, Shojiro, Ogawa, Yuichi (2020) Highly precise characterization of the hydration state upon thermal denaturation of human serum albumin using a 65 GHz dielectric sensor. Physical Chemistry Chemical Physics, 22 (35) 19468-19479 doi:10.1039/d0cp02265a

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Reference TypeJournal (article/letter/editorial)
TitleHighly precise characterization of the hydration state upon thermal denaturation of human serum albumin using a 65 GHz dielectric sensor
JournalPhysical Chemistry Chemical Physics
AuthorsShiraga, KeiichiroAuthor
Urabe, MakoAuthor
Matsui, TakeshiAuthor
Kikuchi, ShojiroAuthor
Ogawa, YuichiAuthor
Year2020Volume22
Issue35
PublisherRoyal Society of Chemistry (RSC)
DOIdoi:10.1039/d0cp02265aSearch in ResearchGate
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Mindat Ref. ID13749901Long-form Identifiermindat:1:5:13749901:6
GUID0
Full ReferenceShiraga, Keiichiro, Urabe, Mako, Matsui, Takeshi, Kikuchi, Shojiro, Ogawa, Yuichi (2020) Highly precise characterization of the hydration state upon thermal denaturation of human serum albumin using a 65 GHz dielectric sensor. Physical Chemistry Chemical Physics, 22 (35) 19468-19479 doi:10.1039/d0cp02265a
Plain TextShiraga, Keiichiro, Urabe, Mako, Matsui, Takeshi, Kikuchi, Shojiro, Ogawa, Yuichi (2020) Highly precise characterization of the hydration state upon thermal denaturation of human serum albumin using a 65 GHz dielectric sensor. Physical Chemistry Chemical Physics, 22 (35) 19468-19479 doi:10.1039/d0cp02265a
In(2020) Physical Chemistry Chemical Physics Vol. 22 (35) Royal Society of Chemistry (RSC)

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Shiraga, Keiichiro, Tanaka, Koichiro, Arikawa, Takashi, Saito, Shinji, Ogawa, Yuichi (2018) Reconsideration of the relaxational and vibrational line shapes of liquid water based on ultrabroadband dielectric spectroscopy. Physical Chemistry Chemical Physics, 20 (41). 26200-26209 doi:10.1039/c8cp04778b
Shiraga, Keiichiro, Suzuki, Tetsuhito, Kondo, Naoshi, Tajima, Takuro, Nakamura, Masahito, Togo, Hiroyoshi, Hirata, Akihiko, Ajito, Katsuhiro, Ogawa, Yuichi (2015) Broadband dielectric spectroscopy of glucose aqueous solution: Analysis of the hydration state and the hydrogen bond network. The Journal of Chemical Physics, 142 (23). 234504pp. doi:10.1063/1.4922482
Kikuchi, Shojiro, Yamashige, Yoshihisa, Hosoki, Ryosuke, Harata, Masahiko, Ogawa, Yuichi (2023) Near-field sensor array with 65-GHz CMOS oscillators can rapidly and comprehensively evaluate drug susceptibility of Mycobacterium. Scientific Reports, 13 (1) doi:10.1038/s41598-023-30873-9
Shiraga, Keiichiro, Adachi, Aya, Ogawa, Yuichi (2017) Characterization of the hydrogen-bond network of water around sucrose and trehalose: H-O-H bending analysis. Chemical Physics Letters, 678. 59-64 doi:10.1016/j.cplett.2017.04.023
Matsarskaia, Olga, BĂĽhl, Lena, Beck, Christian, Grimaldo, Marco, Schweins, Ralf, Zhang, Fajun, Seydel, Tilo, Schreiber, Frank, Roosen-Runge, Felix (2020) Evolution of the structure and dynamics of bovine serum albumin induced by thermal denaturation. Physical Chemistry Chemical Physics, 22 (33) 18507-18517 doi:10.1039/d0cp01857k
Morita, Miho, Matsumura, Fumiki, Shikata, Toshiyuki, Ogawa, Yuichi, Kondo, Naoshi, Shiraga, Keiichiro (2022) Hydrogen-Bond Configurations of Hydration Water around Glycerol Investigated by HOH Bending and OH Stretching Analysis. The Journal of Physical Chemistry B, 126 (47) 9871-9880 doi:10.1021/acs.jpcb.2c05445
Shiraga, Keiichiro, Adachi, Aya, Nakamura, Masahito, Tajima, Takuro, Ajito, Katsuhiro, Ogawa, Yuichi (2017) Characterization of the hydrogen-bond network of water around sucrose and trehalose: Microwave and terahertz spectroscopic study. The Journal of Chemical Physics, 146 (10). 105102pp. doi:10.1063/1.4978232
Pal, Saikat, Pyne, Partha, Samanta, Nirnay, Ebbinghaus, Simon, Mitra, Rajib Kumar (2020) Thermal stability modulation of the native and chemically-unfolded state of bovine serum albumin by amino acids. Physical Chemistry Chemical Physics, 22 (1). 179-188 doi:10.1039/c9cp04887a
Shiraga, Keiichiro, Naito, Hirotaka, Suzuki, Tetsuhito, Kondo, Naoshi, Ogawa, Yuichi (2015) Hydration and Hydrogen Bond Network of Water during the Coil-to-Globule Transition in Poly(N-isopropylacrylamide) Aqueous Solution at Cloud Point Temperature. The Journal of Physical Chemistry B, 119 (17). 5576-5587 doi:10.1021/acs.jpcb.5b01021
Precupas, Aurica, Sandu, Romica, Popa, Vlad T. (2016) Quercetin Influence on Thermal Denaturation of Bovine Serum Albumin. The Journal of Physical Chemistry B, 120 (35). 9362-9375 doi:10.1021/acs.jpcb.6b06214
Dmitriev, A. V., Fedoseev, A. I., Lushnikov, S. G. (2020) Mandelstam–Brillouin Light Scattering in Bovine Serum Albumin Solutions with Different Concentrations in the Vicinity of Thermal Denaturation. Technical Physics, 65 (10) 1546-1550 doi:10.1134/s1063784220100059
 
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