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Marked stepwise differences within a common kinetic mechanism characterize TATA-binding protein interactions with two consensus promoters.

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DNA bends in TATA-binding protein-TATA complexes in solution are DNA sequence-dependent.

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DNA sequence-dependent differences in TATA-binding protein-induced DNA bending in solution are highly sensitive to osmolytes.

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Near-ultraviolet magnetic circular dichroism spectroscopy of protein conformational states: correlation of tryptophan band position and intensity with hemoglobin allostery.

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Related Experiment Videos

Kinetics of association and dissociation phenomena in human hemoglobin studied in a laser light-scattering

Related Concept Videos

Time-resolved fluorescence resonance energy transfer studies of DNA bending in double-stranded oligonucleotides and in DNA-protein complexes.

Marked stepwise differences within a common kinetic mechanism characterize TATA-binding protein interactions with two consensus promoters.

DNA bends in TATA-binding protein-TATA complexes in solution are DNA sequence-dependent.

DNA sequence-dependent differences in TATA-binding protein-induced DNA bending in solution are highly sensitive to osmolytes.

Near-ultraviolet magnetic circular dichroism spectroscopy of protein conformational states: correlation of tryptophan band position and intensity with hemoglobin allostery.

Intermediate species possessing bent DNA are present along the pathway to formation of a final TBP-TATA complex.

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Kinetics of association and dissociation phenomena in human hemoglobin studied in a laser light-scattering...

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Kinetics of association and dissociation phenomena in human hemoglobin studied in a laser light-scattering