找回密码
 To register

QQ登录

只需一步,快速开始

扫一扫,访问微社区

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

[复制链接]
查看: 20965|回复: 38
发表于 2025-3-21 16:43:33 | 显示全部楼层 |阅读模式
书目名称Mechanism of Functional Expression of F1-ATPase
编辑Masahiro Kinoshita
视频video
概述Presents a new view of the mechanism of functional expression of ATP-driven motors.Elucidates four cases on the rotation of the central shaft in F1-ATPase in a unified theory.Explains ideas in straigh
丛书名称SpringerBriefs in Molecular Science
图书封面Titlebook: Mechanism of Functional Expression of F1-ATPase;  Masahiro Kinoshita Book 2021 The Author(s), under exclusive license to Springer Nature Si
描述.This book presents a new view of the mechanism of functional expression of ATP-driven motors (proteins or protein complexes). It is substantially different from the prevailing idea that the motor converts chemical energy to mechanical work. To facilitate understanding, the differences between the new and prevailing views are explained using many illustrations. The book is of interest to those who are not convinced of the notion of chemo–mechanical coupling. The claims presented are the following: The system, which comprises not only the motor but also water, does no mechanical work during the ATP hydrolysis cycle; a protein is moved or a protein in the complex is rotated by the entropic force generated by water. The highlight of the explanation in the book is that the mechanism of unidirectional rotation of the central shaft in F.1.-ATPase is discussed in detail on the basis of this new view. The hydration entropy of each β subunit to which a specific chemical compound (ATP, 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..
出版日期Book 2021
关键词ATP-Driven Motor; F1-ATPase; ATP Hydrolysis Cycle; Water-Entropy Effect; Entropic Force
版次1
doihttps://doi.org/10.1007/978-981-33-6232-1
isbn_softcover978-981-33-6234-5
isbn_ebook978-981-33-6232-1Series ISSN 2191-5407 Series E-ISSN 2191-5415
issn_series 2191-5407
copyrightThe Author(s), under exclusive license to Springer Nature Singapore Pte Ltd. 2021
The information of publication is updating

书目名称Mechanism of Functional Expression of F1-ATPase影响因子(影响力)




书目名称Mechanism of Functional Expression of F1-ATPase影响因子(影响力)学科排名




书目名称Mechanism of Functional Expression of F1-ATPase网络公开度




书目名称Mechanism of Functional Expression of F1-ATPase网络公开度学科排名




书目名称Mechanism of Functional Expression of F1-ATPase被引频次




书目名称Mechanism of Functional Expression of F1-ATPase被引频次学科排名




书目名称Mechanism of Functional Expression of F1-ATPase年度引用




书目名称Mechanism of Functional Expression of F1-ATPase年度引用学科排名




书目名称Mechanism of Functional Expression of F1-ATPase读者反馈




书目名称Mechanism of Functional Expression of F1-ATPase读者反馈学科排名




单选投票, 共有 1 人参与投票
 

1票 100.00%

Perfect with Aesthetics

 

0票 0.00%

Better Implies Difficulty

 

0票 0.00%

Good and Satisfactory

 

0票 0.00%

Adverse Performance

 

0票 0.00%

Disdainful Garbage

您所在的用户组没有投票权限
发表于 2025-3-21 21:14:00 | 显示全部楼层
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.
发表于 2025-3-22 03:54:56 | 显示全部楼层
发表于 2025-3-22 06:07:42 | 显示全部楼层
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.
发表于 2025-3-22 09:04:02 | 显示全部楼层
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.
发表于 2025-3-22 15:05:30 | 显示全部楼层
发表于 2025-3-22 19:32:58 | 显示全部楼层
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
发表于 2025-3-22 21:21:59 | 显示全部楼层
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
发表于 2025-3-23 01:41:28 | 显示全部楼层
https://doi.org/10.1007/978-981-33-6232-1ATP-Driven Motor; F1-ATPase; ATP Hydrolysis Cycle; Water-Entropy Effect; Entropic Force
发表于 2025-3-23 09:28:10 | 显示全部楼层
978-981-33-6234-5The Author(s), under exclusive license to Springer Nature Singapore Pte Ltd. 2021
 关于派博传思  派博传思旗下网站  友情链接
派博传思介绍 公司地理位置 论文服务流程 影响因子官网 SITEMAP 大讲堂 北京大学 Oxford Uni. Harvard Uni.
发展历史沿革 期刊点评 投稿经验总结 SCIENCEGARD IMPACTFACTOR 派博系数 清华大学 Yale Uni. Stanford Uni.
|Archiver|手机版|小黑屋| 派博传思国际 ( 京公网安备110108008328) GMT+8, 2025-6-2 08:24
Copyright © 2001-2015 派博传思   京公网安备110108008328 版权所有 All rights reserved
快速回复 返回顶部 返回列表