Modeled an universal step of ATP hydrolysis by proteins. Out in @ACSCentSci the kinetics of 'inward vs outward product release' path in V1-ATPase. With https://t.co/femFZuATWZ + https://t.co/oQD3PfMVSY, now we have now simulated the complete ROTATORY CATALYSIS cycle !! (1/2) https://t.co/eQ010UsZBw https://t.co/O6W8Hs7kHZ
Chemomechanical Coupling in Hexameric Protein-Protein Interfaces Harnesses Energy within V-Type ATPases.
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Jun 2017 – Jun 2022Where it's discussed
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X / Twitter5 posts
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News5 articles
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YouTube2 videos
AI synopsis
What people are saying
The discussions primarily focus on the technical achievements, such as modeling ATP hydrolysis and the simulation of the rotatory cycle, with words like 'universal step', 'complete cycle', and exclamation marks emphasizing excitement and perceived importance. This indicates a high level of interest and appreciation for the research's contribution to the field.
The overall tone indicates strong support and recognition of the significance of the research, especially with phrases like 'simulated the complete ROTATORY CATALYSIS cycle !!'.
Many discussions highlight fascination with the detailed modeling of ATP hydrolysis, showing high curiosity about the mechanistic aspects.
Posts delve into specifics such as the simulation of the entire rotational cycle, demonstrating a moderate level of engagement beyond superficial interest.
The language suggests that the findings are viewed as meaningful advancements in understanding enzyme mechanics, which could influence further research.
Abstract in brief
- The study investigates how ATP hydrolysis energy is converted into mechanical work in V-type ATPases through conformational changes at protein-protein interfaces, particularly focusing on the Vring structure.
- Using advanced simulation techniques, researchers found that ATP hydrolysis primarily drives the rotation of the central stalk, with the rate of this process influenced by the mechanical properties of the stalk itself.
- The research outlines a detailed sequence of events—ADP and Pi release, ATP binding, and torque generation—highlighting intermediate states that have been confirmed through crystallography, deepening understanding of the enzyme's molecular mechanism.
Top posts
Most liked on X and BlueskyRT @abhisekhsingha1: Modeled an universal step of ATP hydrolysis by proteins. Out in @ACSCentSci the kinetics of 'inward vs outward product…
RT @abhisekhsingha1: Modeled an universal step of ATP hydrolysis by proteins. Out in @ACSCentSci the kinetics of 'inward vs outward product…
RT @abhisekhsingha1: Modeled an universal step of ATP hydrolysis by proteins. Out in @ACSCentSci the kinetics of 'inward vs outward product…
All mentions
Mechanism of Stalk Rotation in V-Type ATPases Explored
This study investigates how ATP hydrolysis converts chemical energy into mechanical work in V-type ATPases, focusing on conformational changes and the role of the Vring structure. Advanced simulations reveal the…
Mechanism of Rotatory Catalysis in V-Type ATPase Enzymes
This study explores how ATP hydrolysis drives the rotation of the central stalk in V-type ATPases, converting chemical energy into mechanical work through conformational changes at protein interfaces, primarily focusing…
RT @abhisekhsingha1: Modeled an universal step of ATP hydrolysis by proteins. Out in @ACSCentSci the kinetics of 'inward vs outward product…
RT @abhisekhsingha1: Modeled an universal step of ATP hydrolysis by proteins. Out in @ACSCentSci the kinetics of 'inward vs outward product…
RT @abhisekhsingha1: Modeled an universal step of ATP hydrolysis by proteins. Out in @ACSCentSci the kinetics of 'inward vs outward product…
RT @abhisekhsingha1: Modeled an universal step of ATP hydrolysis by proteins. Out in @ACSCentSci the kinetics of 'inward vs outward product…
Modeled an universal step of ATP hydrolysis by proteins. Out in @ACSCentSci the kinetics of 'inward vs outward product release' path in V1-ATPase. With https://t.co/femFZuATWZ + https://t.co/oQD3PfMVSY, now we have now simulated the complete ROTATORY CATALYSIS cycle !! (1/2) https://t.co/eQ010UsZBw https://t.co/O6W8Hs7kHZ
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