Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2003-3-5
pubmed:abstractText
With every step it takes, the kinesin motor undergoes a mechanochemical reaction cycle that includes the hydrolysis of one ATP molecule, ADPP(i) release, plus an unknown number of additional transitions. Kinesin velocity depends on both the magnitude and the direction of the applied load. Using specialized apparatus, we subjected single kinesin molecules to forces in differing directions. Sideways and forward loads up to 8 pN exert only a weak effect, whereas comparable forces applied in the backward direction lead to stall. This strong directional bias suggests that the primary working stroke is closely aligned with the microtubule axis. Sideways loads slow the motor asymmetrically, but only at higher ATP levels, revealing the presence of additional, load-dependent transitions late in the cycle. Fluctuation analysis shows that the cycle contains at least four transitions, and confirms that hydrolysis remains tightly coupled to stepping. Together, our findings pose challenges for models of kinesin motion.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-10408448, http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-10617199, http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-11025662, http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-11025663, http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-11427717, http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-12080136, http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-12360289, http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-12368902, http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-14732153, http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-3123999, http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-3926325, http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-7548087, http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-7831332, http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-7854446, http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-7991536, http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-8206961, http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-8413650, http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-8824454, http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-9237757, http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-9237758, http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-9238012, http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-9336196, http://linkedlifedata.com/resource/pubmed/commentcorrection/12591957-9751903
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
100
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2351-6
pubmed:dateRevised
2011-9-26
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Probing the kinesin reaction cycle with a 2D optical force clamp.
pubmed:affiliation
Department of Biological Sciences, Stanford University, Stanford, CA 94305, USA. sblock@stanford.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't