Force production by single kinesin motors

Mark J. Schnitzer, Koen Visscher, Steven M. Block

Research output: Contribution to journalArticle

407 Scopus citations

Abstract

Motor proteins such as kinesin, myosin and polymerase convert chemical energy into work through a cycle that involves nucleotide hydrolysis. Kinetic rates in the cycle that depend upon load identify transitions at which structural changes, such as power strokes or diffusive motions, are likely to occur. Here we show, by modelling data obtained with a molecular force clamp, that kinesin mechanochemistry can be characterized by a mechanism in which a load-dependent isomerization follows ATP binding. This model quantitatively accounts for velocity data over a wide range of loads and ATP levels, and indicates that movement may be accomplished through two sequential 4-nm substeps. Similar considerations account for kinesin processivity, which is found to obey a load-dependent Michaelis-Menten relationship.

Original languageEnglish (US)
Pages (from-to)718-723
Number of pages6
JournalNature Cell Biology
Volume2
Issue number10
DOIs
StatePublished - Oct 1 2000

ASJC Scopus subject areas

  • Cell Biology

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