scholarly journals Estimating π binding energy of N-Heterocyclic carbenes: The role of polarization

2015 ◽  
Vol 36 (8) ◽  
pp. 564-572 ◽  
Author(s):  
Elixabete Rezabal ◽  
Gilles Frison
Keyword(s):  
Binding Energy ◽  
Heterocyclic Carbenes

Role of relativistic and binding-energy effects in the Pb K-shell ionisation by Cl projectiles

1981 ◽  
Vol 87 (1-2) ◽  
pp. 24-26 ◽  
Author(s):  
K.E. Stiebing ◽  
I. Tserruya ◽  
K. Bethge ◽  
H. Schmidt-Böcking
Keyword(s):  
Binding Energy

scholarly journals Structural and Dynamic Characterizations Highlight the Deleterious Role of SULT1A1 R213H Polymorphism in Substrate Binding

2019 ◽  
Vol 20 (24) ◽  
pp. 6256 ◽  
Author(s):  
Raju Dash ◽  
Md. Chayan Ali ◽  
Nayan Dash ◽  
Md. Abul Kalam Azad ◽  
S. M. Zahid Hosen ◽  
...  
Keyword(s):  
Binding Energy ◽  
Cancer Progression ◽  
Conformational Changes ◽  
Substrate Binding ◽  
Dynamics Simulation ◽  
Loss Of Function ◽  
Functional Consequences ◽  
Binding Energy Analysis ◽  
Exogenous Compounds

Sulfotransferase 1A1 (SULT1A1) is responsible for catalyzing various types of endogenous and exogenous compounds. Accumulating data indicates that the polymorphism rs9282861 (R213H) is responsible for inefficient enzymatic activity and associated with cancer progression. To characterize the detailed functional consequences of this mutation behind the loss-of-function of SULT1A1, the present study deployed molecular dynamics simulation to get insights into changes in the conformation and binding energy. The dynamics scenario of SULT1A1 in both wild and mutated types as well as with and without ligand showed that R213H induced local conformational changes, especially in the substrate-binding loop rather than impairing overall stability of the protein structure. The higher conformational changes were observed in the loop3 (residues, 235–263), turning loop conformation to A-helix and B-bridge, which ultimately disrupted the plasticity of the active site. This alteration reduced the binding site volume and hydrophobicity to decrease the binding affinity of the enzyme to substrates, which was highlighted by the MM-PBSA binding energy analysis. These findings highlight the key insights of structural consequences caused by R213H mutation, which would enrich the understanding regarding the role of SULT1A1 mutation in cancer development and also xenobiotics management to individuals in the different treatment stages.

Role of Binding Energy with Coenzyme A in Catalysis by 3-Oxoacid Coenzyme A Transferase

Biochemistry ◽  
1995 ◽  
Vol 34 (37) ◽  
pp. 11678-11689 ◽  
Author(s):  
Adrian Whitty ◽  
Carol A. Fierke ◽  
William P. Jencks
Keyword(s):  
Binding Energy ◽  
Coenzyme A

scholarly journals Role of selective Bioactive Compounds as an Angiotensin Converting Enzyme Inhibitor

2020 ◽  
Author(s):  
Huma Khan ◽  
Tahir Husain ◽  
Monika Kataria ◽  
Amit Seth ◽  
Md. Zubbair Malik ◽  
...  
Keyword(s):  
Binding Energy ◽  
Bioactive Compounds ◽  
Enzyme Inhibitor ◽  
Chloroform Fraction ◽  
Mortality And Morbidity ◽  
New Horizons ◽  
H Nmr ◽  
Potent Drug ◽  
New Perspective

AbstractHypertension is one of a major reason of mortality and morbidity and it is associated with heart and renal disease. The aim of this study is to find out the antihypertensive role of bioactive compounds from selected medicinal plants targeting ACE molecule which so far is not known. The plants taken in this study were Moringa oleifera, Azadirachta indica, and Hibiscus sabdariffa. The nitric oxide and superoxide scavenging property vary from 39.50% to 68% and 37.67 % to 75.50 %. respectively. The inhibition of ACE activity was found maximally in methanolic extract of A. indica (74 %), followed by H. sabdariffa (73.4%), and least in M. oleifera (71.8 %). The bioactive chloroform fraction was characterized for the presence of compound using standard techniques such as LCMS and NMR (13C-NMR 1H-NMR). The results revealed the presence of beta-sitosterol in M. oleifera, azadiradionolide in A. indica and hibiscitrin in H. sabdariffa. The compounds have shown significant low binding energy for hibiscitrin (−12.3kcal/mol), beta-sitosterol (−11.2kcal/mol) and azadiradionolide (−11.3kcal/mol) indicating the high efficacy of binding on the enzyme. While, binding energy of drug captopril was −5.6kcal/mol & enalpril - 8.1kcal/mol in the same pocket of the ACE molecule. Upon subjecting molecular dynamic simulation results indicated that beta sitosterol complex provided more compactness than the hibiscitrin and azadiradionolide compounds. The current study delivers a new perspective for the drug development against systolic blood pressure regulation and also opens new horizons for considering alternate highly potent drug target for hypertension.

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