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Direct
measurements of kinesin torsional properties
reveal flexible domains and occasional
stalk reversals
during stepping. Gutiérrez-Medina,
Fehr, Block.
PNAS (2009). Click
here for Supplemental
Materials. |
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|
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Force
and premature binding of ADP can regulate
the processivity of individual Eg5 dimers.
Valentine and Block. Biophysical Journal
(2009). Click here for Supplemental
Materials. |
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On
the origin of kinesin limping. Fehr, Gutiérrez-Medina,
Asbury, Block. Biophysical Journal (2009). Click here for Supplemental Materials. |
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Direct
observation of the binding state of the
kinesin head to the microtubule. Guydosh
and Block. Nature (2009). Click here
for Supplemental Materials. |
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Folding
and unfolding single RNA molecules under
tension. Woodside, García-García,
Block. Current Opinion in Chemical
Biology (2008). |
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Single-molecule
studies of RNA polymerase: motoring along.
Herbert, Greenleaf, Block. Annual
Review of Biochemistry (2008). |
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Applied
force reveals mechanistic and energetic
details
of transcription termination. Larson, Greenleaf,
Landick, Block. Cell (2008). Click
here for Cell
Commentary. |
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Direct
observation of hierarchical folding
in single
riboswitch aptamers. Greenleaf, Frieda,
Foster, Woodside, Block. Science (2008).
Click here for Supplemental Materials. |
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Precision
steering of an optical trap by electro-optic
deflection. Valentine, Guydosh, Gutiérrez-Medina,
Fehr, Andreasson, Block. Optics Letters
(2008). |
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Kinesin
steps do not alternate in size. Fehr,
Asbury,
Block. Biophysical Journal: Biophysical
Letters (2008). Click here for Supplemental
Materials. |
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Binding, stepping, tracking, gating,
and limping. Block. Biophysical Journal
(2007). |
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Not
so lame after all: kinesin still walks
with
a hobbled head. Guydosh, Block. JGP (2007). |
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Molecule
by molecule, the physics and chemistry of
life: SMB2007. Block, Larson, Greenleaf,
Herbert, Guydosh, Anthony. Nature Chemical
Biology (2007). |
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High-resolution,
single-molecule measurements of biomolecular
motion. Greenleaf, Woodside, Block. Annual
Review of Biophysics Biomolecular Structure
(2007). |
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Eg5
steps it up! Valentine, Fordyce, and Block.
Cell Division (2006). |
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Direct
measurement of the full, sequence-dependent
folding landscape of a nucleic acid. Woodside,
Anthony, Behnke-Parks, Larizadeh, Herschlag,
and Block. Science (2006). Click here
for
Supplemental Materials. |
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Single-molecule,
motion-based DNA sequencing using RNA polymerase.
Greenleaf and Block. Science (2006).
Click here for
Supplemental Materials. |
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Pulling
on the nascent RNA during transcription
does not alter kinetics of elongation or
ubiquitous pausing. Dalal, Larson, Neuman,
Gelles, Landick, and Block. Molecular Cell
(2006). Click here for Supplemental
Materials. |
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Sequence-resolved
detection of pausing by single RNA polymerase
molecules. Herbert, La Porta, Wong, Mooney,
Neuman, Landick and Block. Cell (2006).
Click here for Supplemental
Materials. Click here for Cell
Commentary. Click here for the Stanford
Report article. |
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Backsteps
induced by nucelotide analogs suggest the
front head of kinesin is gated by strain.
Guydosh and Block. PNAS (2006). Click
here for Supplemental
Materials. |
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|
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Nanomechanical
measurements of the sequence-dependent folding
landscapes of single nucleic acid hairpins.
Woodside, Behnke-Parks, Larizadeh, Travers,
Herschlag, and Block. PNAS (2006). Click
here for Supplemental
Materials. |
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Individual
dimers of the mitotic kinesin motor Eg5
step processively and support substantial
loads in vitro. Valentine, Fordyce,
Krzysiak, Gilbert and Block. Nature Cell
Biology (2006). Click here for Supplemental
Materials. |
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