{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Balci H"],"funding":["NIAMS NIH HHS","NIGMS NIH HHS"],"pagination":["413-7"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC1366541"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["89(1)"],"pubmed_abstract":["Myosin VI walks in a hand-over-hand fashion with an average step size of 30 nm, which is much larger than its 10 nm lever arm. Recent experiments suggest that the myosin VI structure has an unfolded and flexible region in the proximal tail which makes such a large step possible. In addition, cryoelectron microscopy images of actomyosin VI show the two heads bound to the actin monomers with a broad distribution of distances, including some as close as a few nanometers. This observation, when combined with the existence of a flexible region in the structure, which takes part in stepping, challenged the hand-over-hand model. In the hand-over-hand model, the lever arm is considered to be rigid and the interhead separation should not be very different from 30 nm. We considered an alternative mo"],"journal":["Biophysical journal"],"pubmed_title":["Interhead distance measurements in myosin VI via SHRImP support a simplified hand-over-hand model."],"pmcid":["PMC1366541"],"funding_grant_id":["R01 AR048931","GM68625","AR44420","R29 AR044420","R01 GM065367","AR48931","R01 GM068625","R01 AR044420"],"pubmed_authors":["Sweeney HL","Balci H","Selvin PR","Ha T"],"additional_accession":[]},"is_claimable":false,"name":"Interhead distance measurements in myosin VI via SHRImP support a simplified hand-over-hand model.","description":"Myosin VI walks in a hand-over-hand fashion with an average step size of 30 nm, which is much larger than its 10 nm lever arm. Recent experiments suggest that the myosin VI structure has an unfolded and flexible region in the proximal tail which makes such a large step possible. In addition, cryoelectron microscopy images of actomyosin VI show the two heads bound to the actin monomers with a broad distribution of distances, including some as close as a few nanometers. This observation, when combined with the existence of a flexible region in the structure, which takes part in stepping, challenged the hand-over-hand model. In the hand-over-hand model, the lever arm is considered to be rigid and the interhead separation should not be very different from 30 nm. We considered an alternative mo","dates":{"release":"2005-01-01T00:00:00Z","publication":"2005 Jul","modification":"2025-04-19T20:54:37.97Z","creation":"2019-03-27T01:25:54Z"},"accession":"S-EPMC1366541","cross_references":{"pubmed":["15863481"],"doi":["10.1529/biophysj.105.060608"]}}