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.

10.1073/pnas.1617873114 http://scihub22266oqcxt.onion/10.1073/pnas.1617873114 C5465881!5465881!28507157     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28507157&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Proc+Natl+Acad+Sci+U+S+A 2017 ; 114 (22): E4399-407 Nephropedia Template TP {{tp|p=28507157|t=2017. Translation and folding of single proteins in real time |pdf=|usr=}}{{28507157}} gab.com Text Translation and folding of single proteins in real time JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28507157 #FOAvip How proteins fold natively with efficient fidelity while being synthesized remains largely unexplored. Understanding protein synthesis on a single-molecule level is of particular interest to the life sciences and relevant for various diseases. Although protein synthesis and folding are well-studied subjects, cotranslational folding has been proven difficult to observe. Using optical tweezers, we measured the mechanics of synthesis and simultaneous folding in real time. We found that cotranslational folding occurs at predictable locations, exerting forces on the nascent polypeptide. Furthermore, we show that transient pauses and gradual slowing of translation occur in particular locations along the protein sequence, facilitating native secondary-structure formation. Thus, the rate of synthesis is inherently coupled to cotranslational folding, assuring reliable and fast native folding. Twit Text FOAVip Translation and folding of single proteins in real time ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28507157 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28507157 #FOAvip English Wikipedia <ref>{{Cite pmid|28507157}}</ref> Translation and folding of single proteins in real time #MMPMID28507157 Wruck F; Katranidis A; Nierhaus KH; Büldt G; Hegner M Proc Natl Acad Sci U S A 2017[May]; 114 (22): E4399-407 PMID28507157show ga How proteins fold natively with efficient fidelity while being synthesized remains largely unexplored. Understanding protein synthesis on a single-molecule level is of particular interest to the life sciences and relevant for various diseases. Although protein synthesis and folding are well-studied subjects, cotranslational folding has been proven difficult to observe. Using optical tweezers, we measured the mechanics of synthesis and simultaneous folding in real time. We found that cotranslational folding occurs at predictable locations, exerting forces on the nascent polypeptide. Furthermore, we show that transient pauses and gradual slowing of translation occur in particular locations along the protein sequence, facilitating native secondary-structure formation. Thus, the rate of synthesis is inherently coupled to cotranslational folding, assuring reliable and fast native folding. äTranslation and folding of single proteins in real time (epmc).pdf DeepDyve Pubget Overpricing