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Size and Shape of Protein Molecules at the Nanometer Level Determined by Sedimentation, Gel Filtration, and Electron Microscopy
  • H. Erickson
  • Materials Science, Medicine
  • Biological Procedures Online
  • 15 May 2009
This review collects a number of simple calculations that are useful for thinking about protein structure at the nanometer level, including the Perrin equation, based on the measured sedimentation coefficient and the calculated maximum S to estimate if a protein is globular or elongated. Expand
Dynamic instability of individual microtubules analyzed by video light microscopy: rate constants and transition frequencies
The data demonstrate that microtubules assembled from pure tubulin undergo dynamic instability over a twofold range of tubulin concentrations, and that the dynamic instability of the plus and minus ends of microtubule can be significantly different. Expand
FtsZ in Bacterial Cytokinesis: Cytoskeleton and Force Generator All in One
Light microscope observations of how Z rings assemble in bacteria are reviewed, and evidence of how FtsZ generates a constriction force: by protofilament bending into a curved conformation is discussed. Expand
Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers.
The similarity of polymers formed by FtsZ and tubulin implies that the protofilament sheet is an ancient cytoskeletal system, originally functioning in bacterial cell division and later modified to make microtubules. Expand
The Symmetrical Structure of Structural Maintenance of Chromosomes (SMC) and MukB Proteins: Long, Antiparallel Coiled Coils, Folded at a Flexible Hinge
The SMC molecule has two complete and identical functional domains at the ends of the long arms, so the bifunctional symmetry and a possible scissoring action at the hinge should provide unique biomechanical properties to the SMC proteins. Expand
Reconstitution of Contractile FtsZ Rings in Liposomes
This work has constructed a membrane-targeted FtsZ (FtsZ-mts) by splicing an amphipathic helix to its C terminus, and found that it formed multiple Z rings that could move laterally in both directions along the length of the liposome and coalesce into brighter Z rings. Expand
Kinetics of protein-protein association explained by Brownian dynamics computer simulation.
The Brownian dynamics simulation method is used to compute the rate of association of neutral spherical model proteins with the stated docking criteria and predicts a rate that is 2000 times faster than that predicted by the simplest geometric calculation and is essentially equal to the rates observed for protein-protein association in aqueous solution. Expand
Condensin and cohesin display different arm conformations with characteristic hinge angles
The visualization of vertebrate condensin and cohesin by electron microscopy shows both complexes display the two-armed structure characteristic of SMC proteins, but their conformations are remarkably different. Expand
The arrangement of the immunoglobulin-like domains of ICAM-1 and the binding sites for LFA-1 and rhinovirus
This analysis suggests that rhinoviruses mimic LFA-1 in binding to the most membrane-distal, and thus most accessible, site of ICAM-1. Expand
Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching
The Z-ring of the mutant ftsZ84, which has 1/10 the guanosine triphosphatase activity of wild-type FtsZ in vitro, showed a 9-fold slower turnover in vivo, implying that assembly dynamics are determined primarily by GTP hydrolysis. Expand