scholarly journals Protein Folding as a Resonance Phenomenon, with Folding Free Energies Determined by Protein-Hydration Shell Interactions

2017 ◽  
Vol 112 (3) ◽  
pp. 52a
Author(s):  
Sungchul Ji
Keyword(s):  
Protein Folding ◽  
Hydration Shell ◽  
Resonance Phenomenon ◽  
Protein Hydration ◽  
Free Energies ◽  
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.

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

Extracting hydrophobic free energies from experimental data: relationship to protein folding and theoretical models

Biochemistry ◽  
1991 ◽  
Vol 30 (40) ◽  
pp. 9686-9697 ◽  
Author(s):  
Kim A. Sharp ◽  
Anthony Nicholls ◽  
Richard Friedman ◽  
Barry Honig
Keyword(s):  
Experimental Data ◽  
Protein Folding ◽  
Theoretical Models ◽  
Free Energies

Structures, binding energies, and thermodynamic functions of NH4+, NH3•+, and their H2O complexes

1993 ◽  
Vol 71 (9) ◽  
pp. 1368-1377 ◽  
Author(s):  
David A. Armstrong ◽  
Arvi Rauk ◽  
Dake Yu
Keyword(s):  
Experimental Data ◽  
Gas Phase ◽  
Thermodynamic Functions ◽  
Hydration Shell ◽  
Binding Energies ◽  
Basis Set ◽  
Free Energies ◽  
Hydrated Complexes ◽  
Optimized Geometries ◽  
First Hydration Shell

Ab initio calculations are performed for [Formula: see text] and [Formula: see text] complexes for n = 0–5. For n = 0 and 1, the geometries of the complexes are optimized at the HF/6-31 + G* and MP2/6-31 + G* levels, and the energies are evaluated at the G2 level. For n = 2–5, the geometry optimizations and frequency calculations are carried out at the HF/6-31 + G* level, and the MP2/6-31 + G* energies are calculated at the HF optimized geometries. Basis set superposition errors are corrected by the Boys–Bernardi scheme at the HF/6-31 + G* level. The gas phase thermodynamic properties [Formula: see text] are evaluated as functions of temperature using standard statistical methods. Based on the calculated binding energies and the thermodynamic functions, the incremental changes in enthalpies and free energies, ΔHn and ΔGn, for the gas phase equilibria (H2O)n−1 M+ + H2O → (H2O)nM+ for M+ = NH4+ and NH3•+, are evaluated in comparison with the experimental data for [Formula: see text] the present results suggest conformations for the hydrated complexes observed in the experiments. The total free energy change for filling the first hydration shell is significantly more negative for NH3•+ than for NH4+.

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