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Dynamical and mechanical study of immobilized microtubules with atomic force microscopy
The dynamics of the assembly/disassembly reaction play an important role in the study of microtubule (MT) polymers. The polymerization rate constant (2±1×10−3 s−1) of this process was determined onExpand
Protein dynamics: imidazole binding to class I C-type cytochromes.
TLDR
The kinetics of imidazole binding are consistent with a change in rate-limiting step at high ligand concentrations for all three proteins, and the movement of the peptide chain in the vicinity of the ligated methionine has been preserved throughout evolution and suggests a role in the function of c-type cytochromes. Expand
Imidazole binding to Rhodobacter capsulatus cytochrome c2. Effect of site-directed mutants on ligand binding.
TLDR
It is found that imidazole binding affinity varies 70-fold, but does not correlate with overall protein stability, and the kinetics of binding are monophasic, which are consistent with localized effects on the dynamics of hinge region 88-102 of the protein, which changes conformation to permit ligand binding. Expand
Protein dynamics in the region of the sixth ligand methionine revealed by studies of imidazole binding to Rhodobacter capsulatus cytochrome c2 hinge mutants.
TLDR
The structure of one of these mutants, G95E, suggests that interactions within the hinge region are stabilized while interaction between the hinge and the heme are destabilized, and appears that these mutations affect the structure of the cytochrome after the hinge area has moved away from the heMe. Expand
Ligand binding and covalent structure of an oxygen-binding heme protein from Rhodobacter sphaeroides, a representative of a new structural family of c-type cytochromes.
TLDR
SHP is thus distantly related to small class I c-type cytochromes but is representative of a distinct family by virtue of its high-spin nature, the lack of a strong sixth ligand, and its capacity to bind oxygen. Expand
Alterations of rings B and C of colchicine are cumulative in overall binding to tubulin but modify each kinetic step.
TLDR
The kinetics of association of ALLO with tubulin is described, where the binding is accompanied by a fluorescence increase with slow biphasic kinetics, indicating binding to fast and slow Tubulin isotypes. Expand
Different kinetic pathways of the binding of two biphenyl analogues of colchicine to tubulin.
TLDR
The kinetics of the interaction of tubulin with two biphenyl analogues of colchicine with 2,3,4-trimethoxy-4'-carbomethoxy-1,1'-biphenyl (TCB) and TKB indicates that these drugs do not discriminate between the isoforms of Tubulin, and the pathway of TCB binding is shown to differ considerably from that of TKB binding. Expand
Evidence for an alternative pathway for colchicine binding to tubulin, based on the binding kinetics of the constituent rings.
TLDR
Stopped-flow kinetic studies reveal that fast TMA binding competes for the initial binding of colchicine, indicating that TMA also binds slowly in a second mode or site and the binding of TMA is practically thermoneutral. Expand
Kinetics of association and dissociation of two enantiomers, NSC 613863 (R)-(+) and NSC 613862 (S)-(-) (CI 980), to tubulin.
TLDR
The kinetics of binding of R- and S-enantiomers were studied by the fluorescence stopped-flow technique and the association rate constant of the S-isomer to the R-site was determined. Expand
Mechanism of tubulin-colchicine recognition: a kinetic study of the binding of the colchicine analogues colchicide and isocolchicine.
TLDR
Competition experiments with MTC give evidence for the existence of a second, slow-reacting low-affinity site for ISO that is not accessible to MTC or MDL. Expand
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