Hydration and dynamics of l-glutamate ion in aqueous solution

2021 ◽  
Author(s):  
Sergej Friesen ◽  
Marina V. Fedotova ◽  
Sergey E. Kruchinin ◽  
Richard Buchner
Keyword(s):  
Aqueous Solution ◽  
Hydration Shell ◽  
Water Dynamics

Dilute l-glutamate affects water dynamics beyond its 1st hydration shell but above 0.4 M only H2O surrounding carboxylate moieties is involved.

scholarly journals Dynamics and mechanism of ultrafast water–protein interactions

2016 ◽  
Vol 113 (30) ◽  
pp. 8424-8429 ◽  
Author(s):  
Yangzhong Qin ◽  
Lijuan Wang ◽  
Dongping Zhong
Keyword(s):  
Protein Interactions ◽  
Hydration Shell ◽  
Water Dynamics ◽  
Side Chain ◽  
Water Molecules ◽  
Ultrafast Dynamics ◽  
Hydration Water ◽  
Water Side ◽  
Dynamics And Function ◽  
And Function

Protein hydration is essential to its structure, dynamics, and function, but water–protein interactions have not been directly observed in real time at physiological temperature to our awareness. By using a tryptophan scan with femtosecond spectroscopy, we simultaneously measured the hydration water dynamics and protein side-chain motions with temperature dependence. We observed the heterogeneous hydration dynamics around the global protein surface with two types of coupled motions, collective water/side-chain reorientation in a few picoseconds and cooperative water/side-chain restructuring in tens of picoseconds. The ultrafast dynamics in hundreds of femtoseconds is from the outer-layer, bulk-type mobile water molecules in the hydration shell. We also found that the hydration water dynamics are always faster than protein side-chain relaxations but with the same energy barriers, indicating hydration shell fluctuations driving protein side-chain motions on the picosecond time scales and thus elucidating their ultimate relationship.

Hydration Shell Structure and Dynamics of Curium(III) in Aqueous Solution: First Principles and Empirical Studies

2011 ◽  
Vol 115 (18) ◽  
pp. 4665-4677 ◽  
Author(s):  
Raymond Atta-Fynn ◽  
Eric J. Bylaska ◽  
Gregory K. Schenter ◽  
Wibe A. de Jong
Keyword(s):  
Aqueous Solution ◽  
First Principles ◽  
Shell Structure ◽  
Empirical Studies ◽  
Hydration Shell ◽  
Structure And Dynamics

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.

Hydration Phenomena in a Concentrated Aqueous Solution of Ce(NO3)3. X-ray Diffraction and Raman Spectroscopy

1983 ◽  
Vol 38 (5) ◽  
pp. 533-539 ◽  
Author(s):  
R. Caminiti ◽  
P. Cucca ◽  
A. D′Andrea
Keyword(s):  
Experimental Data ◽  
Aqueous Solution ◽  
Raman Spectroscopy ◽  
Correlation Function ◽  
Hydration Shell ◽  
X Rays ◽  
X Ray Diffraction ◽  
X Ray ◽  
Experimental Correlation ◽  
Good Agreement

The scattering of X-rays from a concentrated Ce(NO3)3 aqueous solution has been measured and analyzed. The experimental correlation function appears to be mainly characterized by the hydration of the cation: peaks at about 2.55 and 4.65 Å. Good agreement with experimental data is achieved through a model in which the Ce(III) ions have a first and a second hydration shell and also the nitrate group is considered hydrated. Complex formation between cation and anion is confirmed by using Raman spectroscopy.

Protonenübertragungsreaktionen zweibasischer Säuren in wäßriger Lösung: 3-Hydroxypyridin / Proton Transfer Reactions of Dibasic Acids in Aqueous Solution: 3-Hydroxypyridine

1976 ◽  
Vol 31 (5-6) ◽  
pp. 219-224 ◽  
Author(s):  
P. Schuster ◽  
K. Tortschanoff ◽  
H. Winkler
Keyword(s):  
Aqueous Solution ◽  
Relaxation Time ◽  
Proton Transfer ◽  
Aqueous Solutions ◽  
Hydration Shell ◽  
Transfer Reactions ◽  
Diffusion Controlled ◽  
Ultrasound Absorption ◽  
Proton Transfer Reactions

Proton transfer in aqueous solutions of 3-hydroxypyridin (3HP) has been studied by tempera­ture jump relaxation and ultrasound absorption techniques. Two chemical relaxations have been observed. In the range pK1<pH<pK2 the slower of the two processes corresponds to proton transfer between the N and O atoms. A mechanism is proposed which describes the pH and con­centration dependence of the relaxation time measured. Proton transfer involves two types of pro­cesses which operate in parallel: I. pseudomonomolecular, by consecutive diffusion-controlled protonation and deprotonation steps, and 2. bimolecular by diffusion-controlled proton transfer between the neutral 3HP molecule and its corresponding cation or anion. There is no evidence for direct monomolecular proton transfer within the hydration shell of the molecule (k→ ~ k← < 2 × 1O3 sec-1).

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