Site specific point mutation changes specificity: A molecular modeling study by free energy simulations and enzyme kinetics of the thermodynamics in ribonuclease T1 substrate interactions

1993 ◽  
Vol 17 (2) ◽  
pp. 161-175 ◽  
Author(s):  
Arne Elofsson ◽  
Tadeusz Kulinski ◽  
Rudolf Rigler ◽  
Lennart Nilsson
Keyword(s):  
Free Energy ◽  
Molecular Modeling ◽  
Enzyme Kinetics ◽  
Point Mutation ◽  
Specific Point ◽  
Ribonuclease T1 ◽  
Site Specific ◽  
Substrate Interactions ◽  
Energy Simulations ◽  
Kinetics Of

scholarly journals Data on biosynthesis of BPAF glucuronide, enzyme kinetics of BPAF glucuronidation, and molecular modeling

Data in Brief ◽  
2019 ◽  
Vol 22 ◽  
pp. 977-986
Author(s):  
Darja Gramec Skledar ◽  
Jurij Trontelj ◽  
Johanna Troberg ◽  
Tihomir Tomašič ◽  
Anamarija Zega ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
Enzyme Kinetics ◽  
Kinetics Of

Kinetic Aspects of the Interaction of Blood Clotting Enzymes

1968 ◽  
Vol 19 (03/04) ◽  
pp. 364-367 ◽  
Author(s):  
H. C Hemker ◽  
P. W Hemker
Keyword(s):  
Enzyme Kinetics ◽  
Blood Clotting ◽  
Competitive Inhibition ◽  
Competitive Inhibitor ◽  
Kinetics Of

SummaryThe enzyme kinetics of competitive inhibition under conditions prevailing in clotting tests are developed and a method is given to measure relative amounts of a competitive inhibitor by means of the t — D plot.

Prediction of Alkanolamine pKa Values by Combined Molecular Dynamics Free Energy Simulations and ab initio Calculations

2019 ◽  
Author(s):  
Javad Noroozi ◽  
William Smith
Keyword(s):  
Molecular Dynamics ◽  
Free Energy ◽  
Ab Initio Calculations ◽  
Gas Phase ◽  
Quantum Chemical ◽  
Phase Reaction ◽  
Pka Values ◽  
Gas Phase Reaction ◽  
Reaction Free Energy ◽  
Energy Simulations

We use molecular dynamics free energy simulations in conjunction with quantum chemical calculations of gas phase reaction free energy to predict alkanolamines pka values. <br>

Kinetics of Ion-Pair Effect of Aquation of Bromopentaammine Cobalt(III) Complex in Different Dicarboxylate Media

2011 ◽  
Vol 324 ◽  
pp. 166-169 ◽  
Author(s):  
Farah Zeitouni ◽  
Gehan El-Subruiti ◽  
Ghassan Younes ◽  
Mohammad Amira
Keyword(s):  
Free Energy ◽  
Solvent Effect ◽  
Compensation Effect ◽  
Ion Pairing ◽  
Reaction Rates ◽  
Ion Pair ◽  
Free Energy Of Activation ◽  
Different Types ◽  
Different Temperatures ◽  
Kinetics Of

The rate of aquation of bromopentaammine cobalt(III) ion in the presence of different types of dicarboxylate solutions containing tert-butanol (40% V/V) have been measured spectrophotometrically at different temperatures (30-600°C) in the light of the effects of ion-pairing on reaction rates and mechanism. The thermodynamic and extrathermodynamic parameters of activation have been calculated and discussed in terms of solvent effect on the ion-pair aquation reaction. The free energy of activation ∆Gip* is more or less linearly varied among the studied dicarboxylate ion-pairing ligands indicating the presence of compensation effect between ∆Hip* and ∆Sip*. Comparing the kip values with respect of different buffers at 40% of ter-butanol is introduced.

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