The Shape and Flexibility of Tropomyosin Coiled Coils: Implications for Actin Filament Assembly and Regulation
- 1 January 2010
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 395 (2) , 327-339
- https://doi.org/10.1016/j.jmb.2009.10.060
Abstract
No abstract availableKeywords
Funding Information
- National Institutes of Health (HL36153, HL86655)
This publication has 66 references indexed in Scilit:
- CHARMM: The biomolecular simulation programJournal of Computational Chemistry, 2009
- Modulation of Elasticity in Functionally Distinct Domains of the Tropomyosin Coiled-CoilCellular and Molecular Bioengineering, 2009
- Head–Head and Head–Tail Interaction: A General Mechanism for Switching Off Myosin II Activity in CellsMolecular Biology of the Cell, 2008
- Two-Crystal Structures of Tropomyosin C-Terminal Fragment 176–273: Exposure of the Hydrophobic Core to the Solvent Destabilizes the Tropomyosin MoleculeBiophysical Journal, 2008
- A Computational Study of Nucleosomal DNA FlexibilityBiophysical Journal, 2006
- An Atomic Model of the Unregulated Thin Filament Obtained by X-ray Fiber Diffraction on Oriented Actin-Tropomyosin GelsJournal of Molecular Biology, 1995
- Tropomyosin crystal structure and muscle regulationJournal of Molecular Biology, 1986
- CHARMM: A program for macromolecular energy, minimization, and dynamics calculationsJournal of Computational Chemistry, 1983
- The 14-fold periodicity in α-tropomyosin and the interaction with actinJournal of Molecular Biology, 1976
- Analysis of the primary sequence of α-tropomyosin from rabbit skeletal muscleJournal of Molecular Biology, 1975