Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1016/j.bpj.2014.07.035 http://scihub22266oqcxt.onion/10.1016/j.bpj.2014.07.035 C4190598!4190598!25296319     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biophys+J 2014 ; 107 (7): 1661-8 Nephropedia Template TP {{tp|p=25296319|t=2014. Protein Unfolding by Biological Unfoldases: Insights from Modeling |pdf=|usr=}}{{25296319}} gab.com Text Protein Unfolding by Biological Unfoldases: Insights from Modeling JO: Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=25296319 #FOAvip The molecular determinants of the high efficiency of biological machines like unfoldases (e.g., the proteasome) are not well understood. We propose a model to study protein translocation into the chamber of biological unfoldases represented as a funnel. It is argued that translocation is a much faster way of unfolding a protein than end-to-end stretching, especially in a low-force regime, because it allows for a conformational freedom while concentrating local tension on consecutive regions of a protein chain and preventing refolding. This results in a serial unfolding of the protein structures dominated by unzipping. Thus, pulling against the unfoldase pore is an efficient catalyst of the unfolding reaction. We also show that the presence of the funnel makes the tension along the backbone of the substrate protein nonuniform even when the protein gets unfolded. Hence, the stalling force measured by single-molecule force spectroscopy techniques may be smaller than the traction force of the unfoldase motor. Twit Text FOAVip Protein Unfolding by Biological Unfoldases: Insights from Modeling ????Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=25296319 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25296319 #FOAvip English Wikipedia <ref>{{Cite pmid|25296319}}</ref> Protein Unfolding by Biological Unfoldases: Insights from Modeling #MMPMID25296319 Wojciechowski M; Szymczak P; Carrión-Vázquez M; Cieplak M Biophys J 2014[Oct]; 107 (7): 1661-8 PMID25296319show ga The molecular determinants of the high efficiency of biological machines like unfoldases (e.g., the proteasome) are not well understood. We propose a model to study protein translocation into the chamber of biological unfoldases represented as a funnel. It is argued that translocation is a much faster way of unfolding a protein than end-to-end stretching, especially in a low-force regime, because it allows for a conformational freedom while concentrating local tension on consecutive regions of a protein chain and preventing refolding. This results in a serial unfolding of the protein structures dominated by unzipping. Thus, pulling against the unfoldase pore is an efficient catalyst of the unfolding reaction. We also show that the presence of the funnel makes the tension along the backbone of the substrate protein nonuniform even when the protein gets unfolded. Hence, the stalling force measured by single-molecule force spectroscopy techniques may be smaller than the traction force of the unfoldase motor. äProtein Unfolding by Biological Unfoldases: Insights from Modeling (epmc).pdf DeepDyve Pubget Overpricing