Document Detail


Simulations of multi-directional forced unfolding of titin I27.
MedLine Citation:
PMID:  16290077     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Mechanical resistance of a protein under external force is known to depend on the amino acid sequence, unfolding rate constant, topology and the direction of force applied. To assess the affect of force direction on mechanical resistance, molecular dynamics (MD) simulations of the partial unfolding of titin I27 have been carried out by applying a ramp of force between the N-terminus and the alpha-carbon of each amino acid, respectively. The results arbitrarily place the amino acids in a hierarchy in terms of the time at which an unfolding intermediate is formed. The onset of unfolding is indeed affected by force direction; directions that give maximum leverage (for the A strand to detach) unfold to the intermediate quicker than directions that give least leverage. Moreover, the change in the time taken to reach the intermediate, hence the change in mechanical resistance, can be attributed to beta-strand topology. The simulations indicate that experimentally multi-directional forced unfolding could be used to reveal and study strand topology, and suggests that direction of applied force, topology and mechanical resistance are all closely related.
Authors:
Rudesh D Toofanny; Philip M Williams
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2005-11-14
Journal Detail:
Title:  Journal of molecular graphics & modelling     Volume:  24     ISSN:  1093-3263     ISO Abbreviation:  J. Mol. Graph. Model.     Publication Date:  2006 Mar 
Date Detail:
Created Date:  2006-03-06     Completed Date:  2006-05-11     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  9716237     Medline TA:  J Mol Graph Model     Country:  United States    
Other Details:
Languages:  eng     Pagination:  396-403     Citation Subset:  IM    
Affiliation:
Laboratory of Biophysics and Surface Analysis, School of Pharmacy, The University of Nottingham, Nottingham NG7 2RD, UK.
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MeSH Terms
Descriptor/Qualifier:
Computer Simulation*
Hydrogen Bonding
Mathematics
Microscopy, Atomic Force
Models, Molecular
Muscle Proteins / chemistry,  metabolism*
Protein Denaturation*
Protein Kinases / chemistry,  metabolism*
Protein Structure, Secondary
Spectrum Analysis
Time Factors
Chemical
Reg. No./Substance:
0/Muscle Proteins; 0/connectin; EC 2.7.-/Protein Kinases

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


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