Results 21 to 30 of about 795,957 (364)

In Vivo Function of Hsp90 Is Dependent on ATP Binding and ATP Hydrolysis [PDF]

open access: yesThe Journal of Cell Biology, 1998
Heat shock protein 90 (Hsp90), an abundant molecular chaperone in the eukaryotic cytosol, is involved in the folding of a set of cell regulatory proteins and in the re-folding of stress-denatured polypeptides.
W. Obermann   +4 more
semanticscholar   +4 more sources

Structure of the N-terminal Gyrase B fragment in complex with ADP⋅Pi reveals rigid-body motion induced by ATP hydrolysis.

open access: yesPLoS ONE, 2014
Type II DNA topoisomerases are essential enzymes that catalyze topological rearrangement of double-stranded DNA using the free energy generated by ATP hydrolysis.
Frédéric V Stanger   +2 more
doaj   +2 more sources

Kinetic proofreading at single molecular level: Aminoacylation of tRNA^{Ile} and the role of water as an editor [PDF]

open access: yes, 2013
Proofreading/editing in protein synthesis is essential for accurate translation of information from the genetic code. In this article we present a theoretical investigation of efficiency of a kinetic proofreading mechanism that employs hydrolysis of the ...
Bagchi, Biman, Santra, Mantu
core   +12 more sources

Zooming in on ATP Hydrolysis in F1 [PDF]

open access: yesJournal of Bioenergetics and Biomembranes, 2005
We summarize our current view of the reaction mechanism in F(1)-ATPase as it has emerged from experiment, theory, and computational studies over the last several years. ATP catalysis in the catalytic binding pockets of F(1) takes place without the release of any significant free energy and is efficiently driven by the combined action of two water ...
Klaus Schulten, Markus Dittrich
openaire   +3 more sources

Insights into the regulatory function of the ɛ subunit from bacterial F-type ATP synthases: a comparison of structural, biochemical and biophysical data [PDF]

open access: yesOpen Biology, 2018
ATP synthases catalyse the formation of ATP, the most common chemical energy storage unit found in living cells. These enzymes are driven by an electrochemical ion gradient, which allows the catalytic evolution of ATP by a binding change mechanism.
Alexander Krah   +2 more
doaj   +1 more source

Kinetic and Interaction Studies of Adenosine-5′-Triphosphate (ATP) Hydrolysis with Polyoxovanadates

open access: yesMetals, 2021
The reactivity of polyoxovanadates towards adenosine-5′-triphosphate (ATP) hydrolysis at pH 2, 4, 6 and 7 is reported. Detailed kinetic investigation of ATP hydrolysis in the presence of polyoxovanadates was performed through multinuclear nuclear ...
Francisco de Azambuja   +2 more
doaj   +1 more source

ATP hydrolysis in a marine bacterium [PDF]

open access: yesJournal of Bacteriology, 1978
The membrane-bound adenosine triphosphatase of marine pseudomonad B-16, when solubilized, is able to rebind to depleted membrane residues of the bacterium and to those of Escherichia coli.
P H Calcott, A R Bhatti
openaire   +3 more sources

ATP Binding and Hydrolysis Properties of ABCB10 and Their Regulation by Glutathione. [PDF]

open access: yesPLoS ONE, 2015
ABCB10 (ATP binding cassette sub-family B10) is a mitochondrial inner-membrane ABC transporter. ABCB10 has been shown to protect the heart from the impact of ROS during ischemia-reperfusion and to allow for proper hemoglobin synthesis during erythroid ...
Wei Qiu   +3 more
doaj   +1 more source

Thermodynamics of the ATPase Cycle of GlcV, the Nucleotide-Binding Domain of the Glucose ABC Transporter of Sulfolobus solfataricus [PDF]

open access: yes, 2006
ATP-binding cassette transporters drive the transport of substrates across the membrane by the hydrolysis of ATP. They typically have a conserved domain structure with two membrane-spanning domains that form the transport channel and two cytosolic ...
Albers, Sonja-Verena,   +5 more
core   +9 more sources

Nucleotide exchange is sufficient for Hsp90 functions in vivo

open access: yesNature Communications, 2023
Hsp90 is an essential eukaryotic chaperone that regulates the activity of many client proteins. Current models of Hsp90 function, which include many conformational rearrangements, specify a requirement of ATP hydrolysis.
Michael Reidy   +2 more
doaj   +1 more source

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