Document Detail

Role of Denaturation in Maltose Binding Protein Translocation Dynamics.
MedLine Citation:
PMID:  22429088     Owner:  NLM     Status:  Publisher    
We present a computational study on the driven transport of Maltose Binding Protein (MBP) across nano-channels in the framework of coarse-grained modeling. The work is motivated by recent experiments on voltage driven transport of MBP across nanopores exploring the influence of denaturation on translocation pathways. Our simplified approach allows a statistical mechanical interpretation of the process which may result convenient also to the experiments. More specifically, we identified and characterized short and long channel blockades, associated to the translocation of denaturated and folded MBP conformations respectively. We show that long blockades are related to long stall events where MBP undergoes specific and reproducible structural rearrangements. To clarify the origin of the stalls, the {\sl stick-and-slip} translocation is compared to mechanical unfolding pathways obtained via steered molecular dynamics. This comparison clearly shows translocation pathway to significantly differ from free-space unfolding dynamics and strongly suggests that stalling events are preferentially determined by MBP regions denser of long-range native interactions. This result might constitute a possible criterion to predict a-priori some statistical features of protein translocation from the structural analysis.
Marco Bacci; Mauro Chinappi; Carlo Massimo Casciola; Fabio Cecconi
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-3-19
Journal Detail:
Title:  The journal of physical chemistry. B     Volume:  -     ISSN:  1520-5207     ISO Abbreviation:  -     Publication Date:  2012 Mar 
Date Detail:
Created Date:  2012-3-20     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101157530     Medline TA:  J Phys Chem B     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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