Dynamics of the Hydration Water of Antifreeze Glycoproteins

2016 ◽  
Vol 7 (23) ◽  
pp. 4836-4840 ◽  
Author(s):  
Carien C. M. Groot ◽  
Konrad Meister ◽  
Arthur L. DeVries ◽  
Huib J. Bakker
Keyword(s):  
Hydration Water ◽  
Antifreeze Glycoproteins

scholarly journals Antifreeze glycoproteins from Antarctic fish. Inactivation by borate.

1976 ◽  
Vol 251 (10) ◽  
pp. 3033-3036
Author(s):  
A I Ahmed ◽  
Y Yeh ◽  
Y Y Osuga ◽  
R E Feeney
Keyword(s):  
Antarctic Fish ◽  
Antifreeze Glycoproteins

scholarly journals Successive Crystallization of Organically Templated Uranyl Sulfates: Synthesis and Crystal Structures of [pyH](H3O)[(UO2)3(SO4)4(H2O)2], [pyH]2[(UO2)6(SO4)7(H2O)], and [pyH]2[(UO2)2(SO4)3]

2021 ◽  
Vol 5 (1) ◽  
pp. 5
Author(s):  
Evgeny V. Nazarchuk ◽  
Dmitri O. Charkin ◽  
Oleg I. Siidra
Keyword(s):  
Hydrogen Bonds ◽  
Crystal Structures ◽  
Hydrothermal Treatment ◽  
Mother Liquor ◽  
Hydration Water ◽  
Isothermal Evaporation ◽  
Pyridinium Cations

Three new uranyl sulfates, [pyH](H3O)[(UO2)3(SO4)4(H2O)2] (1), [pyH]2[(UO2)6(SO4)7(H2O)] (2), and [pyH]2[(UO2)2(SO4)3] (3), were produced upon hydrothermal treatment and successive isothermal evaporation. 1 is monoclinic, P21/c, a = 14.3640(13), b = 10.0910(9), c = 18.8690(17) Å, β = 107.795(2), V = 2604.2(4) Å3, R1 = 0.038; 2 is orthorhombic, C2221, a = 10.1992(8), b = 18.5215(14), c = 22.7187(17) Å, V = 4291.7(6) Å3, R1 = 0.030; 3 is orthorhombic, Pccn, a = 9.7998(8), b = 10.0768(8), c = 20.947(2) Å, V = 2068.5(3) Å3, R1 = 0.055. In the structures of 1 and 2, the uranium polyhedra and SO4 tetrahedra share vertices to form ∞3[(UO2)3(SO4)4(H2O)2]2− and ∞3[(UO2)6(SO4)7(H2O)]2− frameworks featuring channels (12.2 × 6.7 Å in 1 and 12.9 × 6.5 Å in 2), which are occupied by pyridinium cations. The structure of 3 is comprised of ∞2[(UO2)2(SO4)3]2− layers linked by hydrogen bonds donated by pyridinium cations. The compounds 1–3 are formed during recrystallization processes, in which the evaporation of mother liquor leads to a stepwise loss of hydration water.

Highly precise characterization of the hydration state upon thermal denaturation of human serum albumin using a 65 GHz dielectric sensor

2020 ◽  
Vol 22 (35) ◽  
pp. 19468-19479 ◽  
Author(s):  
Keiichiro Shiraga ◽  
Mako Urabe ◽  
Takeshi Matsui ◽  
Shojiro Kikuchi ◽  
Yuichi Ogawa
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Thermal Denaturation ◽  
Hydration Water ◽  
Biological Functions ◽  
Dielectric Sensor ◽  
Hydration State ◽  
Precise Characterization

The biological functions of proteins depend on harmonization with hydration water surrounding them.

scholarly journals Cooperative functioning between antifreeze glycoproteins.

1978 ◽  
Vol 253 (19) ◽  
pp. 6669-6672 ◽  
Author(s):  
D.T. Osuga ◽  
F.C. Ward ◽  
Y. Yeh ◽  
R.E. Feeney
Keyword(s):  
Antifreeze Glycoproteins

scholarly journals Hydration-dependent dynamic crossover phenomenon in protein hydration water

2014 ◽  
Vol 90 (4) ◽  
Author(s):  
Zhe Wang ◽  
Emiliano Fratini ◽  
Mingda Li ◽  
Peisi Le ◽  
Eugene Mamontov ◽  
...  
Keyword(s):  
Protein Hydration ◽  
Hydration Water ◽  
Dynamic Crossover
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