ChemInform Abstract: Dynamic Molecular Motions of p-Methylcinnamic Acid Included into β-Cyclodextrin Derivatives: A New Type of Free-Energy Relationship in Complex Formation.

ChemInform ◽  
1990 ◽  
Vol 21 (4) ◽  
Author(s):  
Y. KURODA ◽  
M. YAMADA ◽  
I. TABUSHI
Keyword(s):  
Free Energy ◽  
Complex Formation ◽  
Molecular Motions ◽  
Cyclodextrin Derivatives ◽  
New Type ◽  
Methylcinnamic Acid

scholarly journals Predicting gas selectivity in organic ionic plastic crystals by free energy calculations

RSC Advances ◽  
2021 ◽  
Vol 11 (32) ◽  
pp. 19623-19629
Author(s):  
Vinay S. Kandagal ◽  
Jennifer M. Pringle ◽  
Maria Forsyth ◽  
Fangfang Chen
Keyword(s):  
Free Energy ◽  
Gas Separation ◽  
Free Energy Calculations ◽  
Free Energy Calculation ◽  
Energy Calculation ◽  
Plastic Crystal ◽  
Plastic Crystals ◽  
New Type ◽  
Gas Molecules ◽  
Gas Selectivity

The free energy calculation shows the different free energy changes of the adsorption and absorption of gas molecules into an organic ionic plastic crystal, successfully predicting the gas selectivity of this new type of gas separation material.

Linear free energy relationship rate constants and basicities of N-substituted phenyl glycines in positronium-glycine complex formation

1987 ◽  
Vol 137 (5) ◽  
pp. 471-474 ◽  
Author(s):  
Rongti Chen (Y.T. Chen) ◽  
Jiachang Liang ◽  
Youming Du ◽  
Chun Cao ◽  
Dinzhen Yin ◽  
...  
Keyword(s):  
Free Energy ◽  
Complex Formation ◽  
Rate Constants ◽  
Linear Free Energy Relationship ◽  
Linear Free Energy

scholarly journals Affinity and Specificity of Protein U1A-RNA Complex Formation Based on an Additive Component Free Energy Model

2007 ◽  
Vol 371 (5) ◽  
pp. 1405-1419 ◽  
Author(s):  
Bethany L. Kormos ◽  
Yulia Benitex ◽  
Anne M. Baranger ◽  
David L. Beveridge
Keyword(s):  
Free Energy ◽  
Complex Formation ◽  
Energy Model ◽  
Additive Component ◽  
Free Energy Model ◽  
Rna Complex

scholarly journals Effects of CD4 Binding on Conformational Dynamics, Molecular Motions, and Thermodynamics of HIV-1 gp120

2019 ◽  
Vol 20 (2) ◽  
pp. 260 ◽  
Author(s):  
Yi Li ◽  
Lei Deng ◽  
Li-Quan Yang ◽  
Peng Sang ◽  
Shu-Qun Liu
Keyword(s):  
Free Energy ◽  
Conformational Dynamics ◽  
Md Simulations ◽  
Cell Receptor ◽  
Molecular Motions ◽  
Host Cell Receptor ◽  
Gp120 Core ◽  
Glycoprotein Gp120 ◽  
The Stability ◽  
Hiv 1

Human immunodeficiency virus type-1 (HIV-1) infection is triggered by its envelope (Env) glycoprotein gp120 binding to the host-cell receptor CD4. Although structures of Env/gp120 in the liganded state are known, detailed information about dynamics of the liganded gp120 has remained elusive. Two structural models, the CD4-free gp120 and the gp120-CD4 complex, were subjected to µs-scale multiple-replica molecular dynamics (MD) simulations to probe the effects of CD4 binding on the conformational dynamics, molecular motions, and thermodynamics of gp120. Comparative analyses of MD trajectories in terms of structural deviation and conformational flexibility reveal that CD4 binding effectively suppresses the overall conformational fluctuations of gp120. Despite the largest fluctuation amplitude of the V1/V2 region in both forms of gp120, the presence of CD4 prevents it from approaching the gp120 core. Comparison of the constructed free energy landscapes (FELs) shows that CD4 binding reduces the conformational entropy and conformational diversity while enhancing the stability of gp120. Further comparison of the representative structures extracted from free energy basins/minima of FELs reveals that CD4 binding weakens the reorientation ability of V1/V2 and hence hinders gp120 from transitioning out of the liganded state to the unliganded state. Therefore, locking gp120 conformation via restraining V1/V2 reorientation with small molecules seems to be a promising strategy to control HIV-1 infection. Our computer simulation results support the conformational selection mechanism for CD4 binding to gp120 and facilitate the understanding of HIV-1 immune evasion mechanisms.

scholarly journals A Potentiometric Studies of Ternary Complexes of Co(II), Ni(II), Cu(II) and Zn(II) with Ethylenediaamine-N,N,N1,N1-Tetraacetic Acid and Melonic Acid

2018 ◽  
Vol 34 (6) ◽  
pp. 2782-2788
Author(s):  
Sapna Tomar ◽  
Padma Sikarwar
Keyword(s):  
Free Energy ◽  
Ionic Strength ◽  
Complex Formation ◽  
Ternary Complexes ◽  
Potentiometric Studies ◽  
Tetraacetic Acid ◽  
Complex Formation Equilibria ◽  
Formation Equilibria ◽  
Gibb’S Free Energy ◽  
Made In

Potentiometeric investigation on the complex formation equilibria involving Co(II), Ni(II), Cu(II) & Zn(II) with ethylenediaamine-N,N,N1,N1-tetraacetic acid and melonic acid have been made in solution at three different temps viz. (150, 350, 450C). Important thermodynamic parameters namely, change in Gibb’s free energy (DG0), change in enthalpy (DH0) and change in entropy (DS0) and stability constant have been determined potentiometrically at ionic strength of 0.1 M (KNO3).

Chelating Tendencies of Some N-(2-Acetyl-1,3-Indandione) Trialkyl Ammonium Iodides with Transition Metal Ions

1973 ◽  
Vol 28 (5-6) ◽  
pp. 317-318 ◽  
Author(s):  
M. K. Bachlaus ◽  
K. L. Menaria ◽  
P. Nath
Keyword(s):  
Free Energy ◽  
Complex Formation ◽  
Transition Metal ◽  
Copper Complex ◽  
Dissociation Constants ◽  
Transition Metal Ions ◽  
Iron Complex ◽  
Potentiometric Studies ◽  
Kcal Mole ◽  
The Stability

The ligands T.P.A.I.* and T.B.A.I.** have been synthesised and their dissociation constants are 1.738 · 10-10 and 1.412 · 10-8 respectively. The potentiometric studies show that these reagents form 1 : 1 complex with copper(II) and iron(II). The stability constants of copper complex and iron complex with T.P.A.I. are 6.43 and 6.51 respectively and for T.B.A.I. 4.36 and 4.24 respectively. The free energy of complex formation at 25°C are 8.76 Kcal/mole and 8.87 Kcal/mole for Cu (II)-T.P.A.I. and Fe (II)-T.P.A.I. respectively, whereas the free energy of the Cu (II)-T.B.A.I. and Fe(II)-T.B.A.I. are 5.94 Kcal/mole and 5.78 Kcal/mole respectively.

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