LEADER 00847nam0-2200313---450- 001 990008776700403321 005 20090414111653.0 010 $a0125891504 035 $a000877670 035 $aFED01000877670 035 $a(Aleph)000877670FED01 035 $a000877670 100 $a20081210d1976----km-y0itay50------ba 101 1 $aeng 102 $aUS 105 $aa-------001yy 200 1 $aCell hybrids$fNils R. Ringertz, Robert E. Savage 210 $aNew York$cAcademic Press$d1976 215 $aXIV, 366 p.$cill.$d24 cm 676 $a574.8$v19 700 1$aRingertz,$bNils R.$f<1903- >$0314521 701 1$aSavage,$bRobert E.$0314522 801 0$aIT$bUNINA$gRICA$2UNIMARC 901 $aBK 912 $a990008776700403321 952 $aD 6d 1$b1239/CB1$fDMBBM 959 $aDMBBM 996 $aCell hybrids$9810043 997 $aUNINA LEADER 02863oam 2200517 450 001 9910483680003321 005 20210613104801.0 010 $a981-336-232-4 024 7 $a10.1007/978-981-33-6232-1 035 $a(CKB)5590000000430337 035 $a(DE-He213)978-981-33-6232-1 035 $a(MiAaPQ)EBC6449743 035 $a(PPN)252512480 035 $a(EXLCZ)995590000000430337 100 $a20210613d2021 uy 0 101 0 $aeng 135 $aurnn|008mamaa 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 10$aMechanism of functional expression of f1-atpase /$fMasahiro Kinoshita 205 $a1st ed. 2021. 210 1$aSingapore :$cSpringer,$d[2021] 210 4$d©2021 215 $a1 online resource (XI, 79 p. 41 illus., 40 illus. in color.) 225 1 $aSpringerBriefs in Molecular Science,$x2191-5407 311 $a981-336-234-0 311 $a981-336-231-6 327 $a1. Introduction -- 2. A New View on Mechanism of Functional Expression of an ATP-Driven Motor -- 3. Mechanism of Unidirectional Rotation of ?-Subunit in F1-ATPase -- 4. Concluding Remarks. 330 $aThis book presents a new view of the mechanism of functional expression of ATP-driven motors (proteins or protein complexes). It is substantially different from the prevailing idea that the motor converts chemical energy to mechanical work. To facilitate understanding, the differences between the new and prevailing views are explained using many illustrations. The book is of interest to those who are not convinced of the notion of chemo?mechanical coupling. The claims presented are the following: The system, which comprises not only the motor but also water, does no mechanical work during the ATP hydrolysis cycle; a protein is moved or a protein in the complex is rotated by the entropic force generated by water. The highlight of the explanation in the book is that the mechanism of unidirectional rotation of the central shaft in F1-ATPase is discussed in detail on the basis of this new view. The hydration entropy of each ? subunit to which a specific chemical compound (ATP, ADP and Pi, Pi, or nothing) is bound, the hydration entropy of the ?3?3 complex, and the dependence of the hydration entropy of F1-ATPase on the orientation of the ? subunit play essential roles. 410 0$aSpringerBriefs in Molecular Science,$x2191-5407 606 $aBiochemistry 606 $aChemistry 606 $aBiophysics 615 0$aBiochemistry. 615 0$aChemistry. 615 0$aBiophysics. 676 $a572.793 700 $aKinoshita$b Masahiro$01059440 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bUtOrBLW 906 $aBOOK 912 $a9910483680003321 996 $aMechanism of functional expression of f1-atpase$92848016 997 $aUNINA