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ATP and ADP actin states.
MedLine Citation:
PMID:  23348672     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
This minireview is dedicated to the memory of Henryk Eisenberg and honors his major contributions to many areas of biophysics and to the analysis of macromolecular states and interactions in particular. This work reviews the ATP and ADP states of a ubiquitous protein, actins, and considers the present evidence for and against unique, nucleotide-dependent conformations of this protein. The effects of ATP and ADP on specific structural elements of actins, its loops and clefts, as revealed by mutational, crosslinking, spectroscopic, and EPR methods are discussed. It is concluded that the existing evidence points to dynamic equilibria of these structural elements among various conformational states in both ATP- and ADP-actins, with the nucleotides impacting the equilibria distributions. © 2012 Wiley Periodicals, Inc. Biopolymers 99: 245-256, 2013.
Authors:
Dmitri S Kudryashov; Emil Reisler
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biopolymers     Volume:  99     ISSN:  0006-3525     ISO Abbreviation:  Biopolymers     Publication Date:  2013 Apr 
Date Detail:
Created Date:  2013-01-25     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0372525     Medline TA:  Biopolymers     Country:  United States    
Other Details:
Languages:  eng     Pagination:  245-56     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Wiley Periodicals, Inc.
Affiliation:
Department of Chemistry and Biochemistry, the Ohio State University, Columbus, OH 43210. kudryashov.1@osu.edu.
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