Structural dynamics of myoglobin: an infrared kinetic study of ligand migration in mutants YQR and YQRF

2004 ◽  
Vol 109 (1) ◽  
pp. 41-58 ◽  
Author(s):  
Don C. Lamb ◽  
Alessandro Arcovito ◽  
Karin Nienhaus ◽  
Oleksandr Minkow ◽  
Federica Draghi ◽  
...  
Keyword(s):  
Kinetic Study ◽  
Structural Dynamics ◽  
Ligand Migration

scholarly journals Effect of Occluded Ligand Migration on the Kinetics and Structural Dynamics of Homodimeric Hemoglobin

2020 ◽  
Vol 124 (8) ◽  
pp. 1550-1556
Author(s):  
Hanui Kim ◽  
Jong Goo Kim ◽  
Srinivasan Muniyappan ◽  
Tae Wu Kim ◽  
Sang Jin Lee ◽  
...  
Keyword(s):  
Structural Dynamics ◽  
Ligand Migration

Structural Dynamics of Myoglobin:  Effect of Internal Cavities on Ligand Migration and Binding†

Biochemistry ◽  
2003 ◽  
Vol 42 (32) ◽  
pp. 9647-9658 ◽  
Author(s):  
Karin Nienhaus ◽  
Pengchi Deng ◽  
Jan M. Kriegl ◽  
G. Ulrich Nienhaus
Keyword(s):  
Structural Dynamics ◽  
Internal Cavities ◽  
Ligand Migration

scholarly journals Impact of azole drugs on energetics, kinetics, and ligand migration pathways of CO photo-dissociation in bacterial flavohemoglobins

RSC Advances ◽  
2020 ◽  
Vol 10 (30) ◽  
pp. 17930-17941
Author(s):  
David Butcher ◽  
Myriam Moussaoui ◽  
Laura Baciou ◽  
Jaroslava Miksovska
Keyword(s):  
Structural Dynamics ◽  
Ligand Migration ◽  
Migration Pathways

Impact of ketoconalzole and miconazole on structural dynamics of flavohemoglobin.

Structural dynamics of P-type ATPase ion pumps

2019 ◽  
Vol 47 (5) ◽  
pp. 1247-1257 ◽  
Author(s):  
Mateusz Dyla ◽  
Sara Basse Hansen ◽  
Poul Nissen ◽  
Magnus Kjaergaard
Keyword(s):  
Structural Dynamics ◽  
Single Molecule ◽  
New Technologies ◽  
Atp Hydrolysis ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Time Resolved ◽  
Dynamics Simulations ◽  
Types Of Information ◽  
P Type

Abstract P-type ATPases transport ions across biological membranes against concentration gradients and are essential for all cells. They use the energy from ATP hydrolysis to propel large intramolecular movements, which drive vectorial transport of ions. Tight coordination of the motions of the pump is required to couple the two spatially distant processes of ion binding and ATP hydrolysis. Here, we review our current understanding of the structural dynamics of P-type ATPases, focusing primarily on Ca2+ pumps. We integrate different types of information that report on structural dynamics, primarily time-resolved fluorescence experiments including single-molecule Förster resonance energy transfer and molecular dynamics simulations, and interpret them in the framework provided by the numerous crystal structures of sarco/endoplasmic reticulum Ca2+-ATPase. We discuss the challenges in characterizing the dynamics of membrane pumps, and the likely impact of new technologies on the field.

A kinetic study of controlling nitrogen in process for boron steel by using30N2isotope gas

2008 ◽  
Vol 105 (12) ◽  
pp. 601-608
Author(s):  
Seung Min Han ◽  
Dong Joon Min ◽  
Joo Hyun Park ◽  
Jung Ho Park ◽  
Jong Min Park
Keyword(s):  
Kinetic Study ◽  
Boron Steel

Kinetic Study of the Effect of Heparin on the Amidase Activity of Trypsin, Plasmin and Urokinase

1983 ◽  
Vol 49 (03) ◽  
pp. 199-203 ◽  
Author(s):  
V M Yomtova ◽  
N A Stambolieva ◽  
B M Blagoev
Keyword(s):  
Kinetic Study ◽  
Active Center ◽  
Simultaneous Presence ◽  
Amidase Activity ◽  
Competitive Inhibitors ◽  
Uncompetitive Inhibitor

SummaryIt was found that the effect of heparin on the amidase activity of urokinase (E C 3.4.21.31), plasmin (E C 3.4.21.7) and trypsin (E C 3.4.21.4) depended on the substrate used. No effect of heparin on the amidase activity of urokinase and trypsin was observed when Pyro Glu-Gly-Arg-p-nitroanilide (S-2444) and α-N-acetyl-L-lysine-p-nitroanilide (ALNA) were used as substrates. Heparin acted as a uncompetitive inhibitor of trypsin (Ki = 1.2×10-6 M), plasmin (Ki = 4.9×10-6 M) and urokinase (Ki = l.0×10-7 M) when Bz-Phe-Val-Arg-p-nitroanilide (S-2160), H-D-Val-Leu-Lys-p-nitroanilide (S-2251) and plasminogen, respectively, were used as substrates. These results, as well as the data obtained by studying the effect of the simultaneous presence of heparin and competitive inhibitors suggest that although heparin is not bound at the active center of these enzymes, it may influence the effectivity of catalysis.

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