Protective action of trehalose and glucose on protein hydration shell clarified by using X-ray and neutron scattering

2018 ◽  
Vol 551 ◽  
pp. 249-255 ◽  
Author(s):  
Satoshi Ajito ◽  
Mitsuhiro Hirai ◽  
Hiroki Iwase ◽  
Nobutaka Shimizu ◽  
Noriyuki Igarashi ◽  
...  
Keyword(s):  
Neutron Scattering ◽  
Protective Action ◽  
Hydration Shell ◽  
Protein Hydration ◽  
X Ray ◽  
Protein Hydration Shell

Length-scale dependence of protein hydration-shell density

2020 ◽  
Vol 22 (14) ◽  
pp. 7340-7347
Author(s):  
Akash Deep Biswas ◽  
Vincenzo Barone ◽  
Andrea Amadei ◽  
Isabella Daidone
Keyword(s):  
Hydration Shell ◽  
Scale Dependence ◽  
Protein Hydration ◽  
Length Scale ◽  
Protein Size ◽  
Protein Hydration Shell

An increase in protein hydration-shell density relative to that of the bulk is observed (in the range of 4–14%) for all studied proteins and this density-increment, which decreases for decreasing protein size, is caused by the protein size only.

scholarly journals Quantum Behavior of Water Protons in Protein Hydration Shell

2009 ◽  
Vol 96 (5) ◽  
pp. 1939-1943 ◽  
Author(s):  
S.E. Pagnotta ◽  
F. Bruni ◽  
R. Senesi ◽  
A. Pietropaolo
Keyword(s):  
Hydration Shell ◽  
Protein Hydration ◽  
Quantum Behavior ◽  
Protein Hydration Shell

scholarly journals Proton Momentum Distribution in a Protein Hydration Shell

2007 ◽  
Vol 98 (13) ◽  
Author(s):  
R. Senesi ◽  
A. Pietropaolo ◽  
A. Bocedi ◽  
S. E. Pagnotta ◽  
F. Bruni
Keyword(s):  
Momentum Distribution ◽  
Hydration Shell ◽  
Protein Hydration ◽  
Proton Momentum ◽  
Protein Hydration Shell

The unfolding effects on the protein hydration shell and partial molar volume: a computational study

2016 ◽  
Vol 18 (40) ◽  
pp. 28175-28182 ◽  
Author(s):  
Sara Del Galdo ◽  
Andrea Amadei
Keyword(s):  
Aqueous Solution ◽  
Computational Analysis ◽  
Computational Study ◽  
Hydration Shell ◽  
Partial Molar Volumes ◽  
Globular Proteins ◽  
Protein Hydration ◽  
Native Protein ◽  
Unfolded State ◽  
Protein Hydration Shell

In this paper we apply the computational analysis recently proposed by our group to characterize the solvation properties of a native protein in aqueous solution, and to four model aqueous solutions of globular proteins in their unfolded states thus characterizing the protein unfolded state hydration shell and quantitatively evaluating the protein unfolded state partial molar volumes.

scholarly journals Direct Evidence of Effect of Glycerol on Hydration and Helix-to-Sheet Transition of Myoglobin

2018 ◽  
Author(s):  
M. Hirai ◽  
S. Ajito ◽  
M. Sugiyama ◽  
H. Iwase ◽  
S.-I. Takata ◽  
...  
Keyword(s):  
Neutron Scattering ◽  
Tertiary Structure ◽  
Hydration Shell ◽  
Scattering Data ◽  
Variation Method ◽  
Protein Surface ◽  
X Ray ◽  
X Ray Scattering ◽  
Structural Levels ◽  
Ray Scattering

AbstractBy using wide-angle X-ray scattering (WAXS), small-angle neutron scattering, and theoretical scattering function simulation, we have clarified the effect of glycerol on both the thermal structure transition and the hydration-shell of myoglobin. At the glycerol concentration, ≤ ∼40 % v/v, the decreasing tendency in the maximum dimension and the radius of gyration was observed by X-ray scattering. The neutron scattering result using the inverse contrast variation method directly shows the preservation of the hydration-shell density at the concentration ≤ ∼40 % v/v. This phenomenon is reasonably explained by the preferential exclusion of glycerol from the protein surface to preserve the hydration shell, as suggested by the previous studies. While, at the concentration, ≥ 50 % v/v, the opposite tendency was observed. It suggests the preferential solvation (partial preferential penetration or replacement of glycerol into or with hydration-shell water surrounding the protein surface) occurs at the higher concentration. The observed WAXS scattering data covers the distinct hierarchical structural levels of myoglobin structure ranging from the tertiary structure to the secondary one. Therefore, we have clarified the effect of glycerol on the thermal structural stability myoglobin at different hierarchical structural levels separately. Against the temperature rise, the structural transition temperatures for all hierarchical structural levels were elevated. Especially, the tertiary structure of myoglobin was more stabilized compared with the internal-structure and the helix-to-cross transition. It suggests that the protective action of glycerol on protein structures essentially results from the preservation of the preferential hydration-shell of proteins.

scholarly journals Protein hydration in solution: Experimental observation by x-ray and neutron scattering

1998 ◽  
Vol 95 (5) ◽  
pp. 2267-2272 ◽  
Author(s):  
D. I. Svergun ◽  
S. Richard ◽  
M. H. J. Koch ◽  
Z. Sayers ◽  
S. Kuprin ◽  
...  
Keyword(s):  
Neutron Scattering ◽  
Experimental Observation ◽  
Protein Hydration ◽  
X Ray
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