dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorVale, Ronald D.
dc.creatorMilligan, Ronald A.
dc.date2016-10-26T17:57:25Z
dc.date2016-10-26T17:57:25Z
dc.date.accessioned2017-04-06T12:16:52Z
dc.date.available2017-04-06T12:16:52Z
dc.identifierhttp://acervodigital.unesp.br/handle/unesp/365472
dc.identifierhttp://objetoseducacionais2.mec.gov.br/handle/mec/22539
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/961754
dc.descriptionShows two heads of the kinesin dimer work in a coordinated manner to move processively along the track. The coiled coil (gray) extends towards the top and leads up to the kinesin cargo. Each catalytic core (blue) is bound to a tubulin heterodimer (green, beta subunit; white, alpha subunit) along a microtubule protofilament (the cylindrical microtubule is composed of 13 protofilament tracks). To adopt this position, the neck linker points forward on the trailing head (orange; neck linker next to but not tightly docked to the core) and rearward on the leading head (red). ATP binding to the leading head will initiate neck linker docking. Neck linker docking is completed by the leading head (yellow), which throws the partner head forward by 160 angstroms (arrow) toward the next tubulin binding site. After a random diffusional search, the new leading head docks tightly onto the binding site, which completes the 80 angstrom motion of the attached cargo. Polymer binding also accelerates ADP release, and during this time, the trailing head hydrolyzes ATP to ADP-Pi. After ADP dissociates, an ATP binds to the leading head and the neck linker begins to zipper onto the core (partially docked neck indicated by the orange color). The trailing head, which has released its phosphate (Pi) and detached its neck linker (red) from the core, is in the process of being thrown forward
dc.descriptionComponente Curricular::Educação Superior::Ciências Biológicas::Microbiologia
dc.descriptionComponente Curricular::Educação Superior::Ciências Exatas e da Terra::Química
dc.publisherThe American Society for Cell Biology, ASBC Image & Video Library
dc.relationA Moving Kinesin Motor Protein.mov
dc.rightsYou may use the Images only for research and educational purposes in an educational institution. Images may be stored on a network server, hard drive or removable media, but only while this Agreement remains in effect. All of the Images you use must be accompanied by a notice stating, "© [Date and Author's or Owner's Name]. All rights reserved. Reprinted under license from The American Society for Cell Biology." The notice shall appear with the Images or on a credits page. "Educational purposes" means (i) non-commercial instruction or curriculum based teaching by educators to students at nonprofit educational institutions, (ii) planned non-commercial study, investigation or research directed toward making a contribution to a field of knowledge, or (iii) presentation of research findings at non-commercial peer conferences, workshops or seminars, but in any event there must be express written permission from ASCB before an Image can be published. "Educational institutions" include K-12 schools, colleges and universities. Libraries, museums, hospitals, research institutes and other nonprofit organizations are considered educational institutions when they engage in nonprofit instructional, research or scholarly activities for educational purposes
dc.subjectCell biology
dc.subjectMicrotubule
dc.subjectMotor protein
dc.subjectADP
dc.subjectATP
dc.subjectEducação Superior::Ciências Biológicas::Microbiologia::Biologia e Fisiologia dos Microorganismos
dc.subjectEducação Superior::Ciências Exatas e da Terra::Química::Estrutura, Conformação e Estereoquímica
dc.titleA moving kinesin motor protein
dc.typeOtro


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