Titlebook: Mechanism of Functional Expression of F1-ATPase; Masahiro Kinoshita Book 2021 The Author(s), under exclusive license to Springer Nature Si

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微不足道

A New View on Mechanism of Functional Expression of an ATP-Driven Molecular Motor,nal, configurational entropy of water is a principal component of the system free energy. A protein (e.g., myosin) is moved or a protein in the complex (e.g., the γ subunit in the α.β.γ complex of F.-ATPase) is rotated in the direction where the water entropy already maximized can be retained.

CHOKE

極少

Concluding Remarks,py loss is caused, the structures of the other two portions are reorganized to make up for the loss. We also comment on the rotation mechanism of V.-ATPase which we intend to explore in the next stage.

Enzyme

Appendix 2: Morphometric Approach,eference interaction site model (3D-RISM) theory are applied to processes 1 and 2, respectively, is capable of calculating the hydration free energy, energy, and entropy of a large polyatomic solute like a protein with sufficient accuracy and high speed.

Anthrp

流眼淚

ation and politics has long been overdue. On Rousseau: An Introduction to his Radical Thinking on Education and Politics fills this void, and should interest educators, educators of educators, philosophy students, and all with 978-94-6091-385-3

FRET

2191-5407 ADP and Pi, Pi, or nothing) is bound, the hydration entropy of the α.3.β.3.?complex, and the dependence of the hydration entropy of F.1.-ATPase on the orientation of the γ subunit play essential roles..978-981-33-6234-5978-981-33-6232-1Series ISSN 2191-5407 Series E-ISSN 2191-5415

匯總

https://doi.org/10.1007/978-981-33-6232-1ATP-Driven Motor; F1-ATPase; ATP Hydrolysis Cycle; Water-Entropy Effect; Entropic Force

bronchodilator

978-981-33-6234-5The Author(s), under exclusive license to Springer Nature Singapore Pte Ltd. 2021