A Normal Mode Analysis of Structural Plasticity in the Biomolecular Motor F1-ATPase
- 1 July 2004
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 340 (2), 345-372
- https://doi.org/10.1016/j.jmb.2004.04.044
Abstract
No abstract availableThis publication has 57 references indexed in Scilit:
- Structure of Bovine Mitochondrial F1-ATPase with Nucleotide Bound to All Three Catalytic SitesCell, 2001
- The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution.Nature Structural & Molecular Biology, 2000
- ATP synthase: what we know about ATP hydrolysis and what we do not know about ATP synthesisBiochimica et Biophysica Acta (BBA) - Bioenergetics, 2000
- On what makes the γ subunit spin during ATP hydrolysis by F1Biochimica et Biophysica Acta (BBA) - Bioenergetics, 2000
- Structural changes linked to proton translocation by subunit c of the ATP synthaseNature, 1999
- ATP Synthesis by Rotary Catalysis (Nobel lecture)Angewandte Chemie-International Edition, 1998
- THE ATP SYNTHASE—A SPLENDID MOLECULAR MACHINEAnnual Review of Biochemistry, 1997
- Direct observation of the rotation of F1-ATPaseNature, 1997
- Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondriaNature, 1994
- The binding change mechanism for ATP synthase — Some probabilities and possibilitiesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1993