scholarly journals The Relationship between Enzyme Conformational Change, Proton Transfer, and Phosphoryl Transfer in β-Phosphoglucomutase

ACS Catalysis ◽  
2021 ◽  
pp. 12840-12849
Author(s):  
Angus J. Robertson ◽  
Alex L. Wilson ◽  
Matthew J. Burn ◽  
Matthew J. Cliff ◽  
Paul L. A. Popelier ◽  
...  
Keyword(s):  
Proton Transfer ◽  
Conformational Change ◽  
Phosphoryl Transfer ◽  
The Relationship

scholarly journals A Benchmark Test on the Leapfrog Integrator and its Middle Alternative

2021 ◽  
Author(s):  
Zhaoxi Sun
Keyword(s):  
Free Energy ◽  
Proton Transfer ◽  
Conformational Change ◽  
Equations Of Motion ◽  
Intramolecular Proton Transfer ◽  
Energy Simulation ◽  
Benchmark Test ◽  
Benchmark Tests ◽  
Two Systems ◽  
Simulation Results

<p>Benchmark tests of the integrators are performed on three systems. In the first two systems including the NMA system (ACE-NME) and an AT tract (A7-T7), the conformational change of dihedral flipping is simulated. In the last system malonaldehyde, the intramolecular proton transfer is investigated. The free energy simulation results obtained with two integrators for the equations of motion including the leapfrog (LF) integrator and the leapfrog-middle (LF-middle) scheme are tested extensively.</p>

scholarly journals Critical Role of Substrate Conformational Change in the Proton Transfer Process Catalyzed by 4-Oxalocrotonate Tautomerase

2009 ◽  
Vol 131 (7) ◽  
pp. 2687-2698 ◽  
Author(s):  
J. Javier Ruiz-Pernía ◽  
Mireia Garcia-Viloca ◽  
Sudeep Bhattacharyya ◽  
Jiali Gao ◽  
Donald G. Truhlar ◽  
...  
Keyword(s):  
Proton Transfer ◽  
Conformational Change ◽  
Transfer Process ◽  
Critical Role ◽  
Proton Transfer Process

scholarly journals Trans-dominant inhibition of integrin function.

1996 ◽  
Vol 7 (12) ◽  
pp. 1939-1951 ◽  
Author(s):  
F Díaz-González ◽  
J Forsyth ◽  
B Steiner ◽  
M H Ginsberg
Keyword(s):  
Conformational Change ◽  
Conformational Changes ◽  
Biological Effects ◽  
Focal Adhesions ◽  
Extracellular Domain ◽  
Integrin Signaling ◽  
Conformational Rearrangement ◽  
Integrin Ligands ◽  
The Relationship ◽  
Specific Inhibitors

Occupancy of integrin adhesion receptors can alter the functions of other integrins and cause partition of the ligand-occupied integrin into focal adhesions. Ligand binding also changes the conformation of integrin extracellular domains. To explore the relationship between ligand-induced conformational change and integrin signaling, we examined the effect of ligands specific for integrin alpha IIb beta 3 on the functions of target integrins alpha 5 beta 1 and alpha 2 beta 1. We report that binding of integrin-specific ligands to a suppressive integrin can inhibit the function of other target integrins (trans-dominant inhibition). Trans-dominant inhibition is due to a blockade of integrin signaling. Furthermore, this inhibition involves both a conformational change in the extracellular domain and the presence of the beta cytoplasmic tail in the suppressive integrin. Similarly, ligand-induced recruitment of alpha IIb beta 3 to focal adhesions also involves a conformational rearrangement of its extracellular domain. These findings imply that the ligand-induced conformational changes can propagate from an integrin's extracellular to its intracellular face. Trans-dominant inhibition by integrin ligands may coordinate integrin signaling and can lead to unexpected biological effects of integrin-specific inhibitors.

The relationship between substituent-induced energy and charge effects in proton-transfer equilibriums

1981 ◽  
Vol 103 (6) ◽  
pp. 1344-1349 ◽  
Author(s):  
Warren J. Hehre ◽  
Mare Taagepera ◽  
Robert W. Taft ◽  
Ronald D. Topsom
Keyword(s):  
Proton Transfer ◽  
Charge Effects ◽  
The Relationship
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