Single-molecule fluorescence to study molecular motors

No abstract is available for this paper.

• Publication year

  2007

• Venue

  Quarterly Reviews of Biophysics (print)

• Publication date

  2007-02-01

• Fields of study

  Biology, Medicine, Physics, Chemistry

• Identifiers
  DOI 10.1017/S0033583507004611PMID 17666122
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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  2007cited by this paper
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• Molecular Motors

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• Full-length myosin VI dimerizes and moves processively along actin filaments upon monomer clustering.

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• Extracting dwell time sequences from processive molecular motor data.

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• A flexible domain is essential for the large step size and processivity of myosin VI.

  2005cited by this paper
• Observation of individual microtubule motor steps in living cells with endocytosed quantum dots.

  2005cited by this paper
• ATP hydrolysis cycle–dependent tail motions in cytoplasmic dynein

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• Differential labeling of myosin V heads with quantum dots allows direct visualization of hand-over-hand processivity.

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• Interhead distance measurements in myosin VI via SHRImP support a simplified hand-over-hand model.

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• The unique insert in myosin VI is a structural calcium-calmodulin binding site.

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• Kinesin Walks Hand-Over-Hand

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• Myosin V Walks Hand-Over-Hand: Single Fluorophore Imaging with 1.5-nm Localization

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• Kinesin Moves by an Asymmetric Hand-Over-Hand Mechanism

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• F 1-ATPase Is a Highly Efficient Molecular Motor that Rotates with Discrete 120 8 Steps

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• Kinesin hydrolyses one ATP per 8-nm step

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• Identification of a Microtubule-binding Domain in a Cytoplasmic Dynein Heavy Chain*

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• Materials and Methods Som Text Figs. S1 to S3 References and Notes Kinesin Moves by an Asymmetric Hand-over-hand Mechanism

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