Document Detail


Molecular motors and nonuniform ratchets.
MedLine Citation:
PMID:  11156296     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Dimeric kinesin presumably moves in a "hand-over-hand" fashion via alternating steps of its two heads, which can cooperate in various ways. This motion is discussed in the framework of nonuniform ratchet models in which the molecular motor is described by M internal states and undergoes transitions at K spatial locations within the period of the molecular force potentials. Two subclasses of models with (M, K)=(3, 2) and (M, K)=(2, 2) are studied which correspond to weakly and strongly cooperative heads, respectively. Both subclasses lead to the same universal relationship between the motor velocity and the unbinding rate constant of the motor heads which is reminiscent of, but distinct from, Michaelis-Menten kinetics.
Authors:
R Lipowsky; T Harms
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  European biophysics journal : EBJ     Volume:  29     ISSN:  0175-7571     ISO Abbreviation:  Eur. Biophys. J.     Publication Date:  2000  
Date Detail:
Created Date:  2001-01-11     Completed Date:  2001-03-15     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8409413     Medline TA:  Eur Biophys J     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  542-8     Citation Subset:  IM    
Affiliation:
MPI für Kolloid- und Grenzflächenforschung, Golm, Germany. lipowsky@mpikg-golm.mpg.de
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphate / metabolism
Dimerization
Enzymes / metabolism
Kinesin / chemistry,  physiology*
Kinetics
Models, Theoretical
Molecular Motor Proteins / physiology*
Protein Conformation
Chemical
Reg. No./Substance:
0/Enzymes; 0/Molecular Motor Proteins; 56-65-5/Adenosine Triphosphate; EC 3.6.1.-/Kinesin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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