Use of Photonic Force Microscopy to Study Single-Motor-Molecule Mechanics

S Jeney, E-L Florin, JKH Hoerber

Research output: Chapter in Book/Report/Conference proceedingChapter in a book

9 Citations (Scopus)

Abstract

With the intensive study of functional properties of motor proteins at the single-molecule level, many new insights were gained on the correlation between the kinesin structure and its function. Recent work on kinesins has demonstrated that the neck and the first hinge region of the motor play an important role in kinesin directionality, velocity, and ATPase activity (1-4). The investigation of the three-dimensional (3D) mechanical properties in this context can provide the information to understand how structural changes stipulate the molecular function. A 3D view is essential, as mechanical properties can be anisotropic and motor molecules, in general, move in space to fulfill their function.
Translated title of the contributionUse of Photonic Force Microscopy to Study Single-Motor-Molecule Mechanics
Original languageEnglish
Title of host publicationKinesin Protocols in "Methods in Molecular Biology"
EditorsIsabelle Vernos
PublisherHumano Press Inc. USA
Pages91 - 108
Number of pages18
Volume164
ISBN (Print)0896037665
Publication statusPublished - 2001

Bibliographical note

Other identifier: DOI 10.1226/0896037665

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