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.

10.1146/annurev-biophys-070816-033819 http://scihub22266oqcxt.onion/10.1146/annurev-biophys-070816-033819 C5800964!5800964!28301766     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Annu+Rev+Biophys 2017 ; 46 (ä): 85-103 Nephropedia Template TP {{tp|p=28301766|t=2017. Biophysical models of protein evolution: Understanding the patterns of evolutionary sequence divergence |pdf=|usr=}}{{28301766}} gab.com Text Biophysical models of protein evolution: Understanding the patterns of evolutionary sequence divergence JO: Annu Rev Biophys http://www.kidney.de/pget.php?&tw=1&pmid=28301766 #FOAvip For decades, rates of protein evolution have been interpreted in terms of the vague concept of ?functional importance?. Slowly evolving proteins or sites within proteins were assumed to be more functionally important and thus subject to stronger selection pressure. More recently, biophysical models of protein evolution, which combine evolutionary theory with protein biophysics, have completely revolutionized our view of the forces that shape sequence divergence. Slowly evolving proteins have been found to evolve slowly because of selection against toxic misfolding and misinteractions, linking their rate of evolution primarily to their abundance. Similarly, most slowly evolving sites in proteins are not directly involved in function, but mutating them has large impacts on protein structure and stability. Here, we review the studies of the emergent field of biophysical protein evolution that have shaped our current understanding of sequence divergence patterns. We also propose future research directions to develop this nascent field. Twit Text FOAVip Biophysical models of protein evolution: Understanding the patterns of evolutionary sequence divergence ????Annu Rev Biophys http://www.kidney.de/pget.php?&tw=1&pmid=28301766 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28301766 #FOAvip English Wikipedia <ref>{{Cite pmid|28301766}}</ref> Biophysical models of protein evolution: Understanding the patterns of evolutionary sequence divergence #MMPMID28301766 Echave J; Wilke CO Annu Rev Biophys 2017[May]; 46 (ä): 85-103 PMID28301766show ga For decades, rates of protein evolution have been interpreted in terms of the vague concept of ?functional importance?. Slowly evolving proteins or sites within proteins were assumed to be more functionally important and thus subject to stronger selection pressure. More recently, biophysical models of protein evolution, which combine evolutionary theory with protein biophysics, have completely revolutionized our view of the forces that shape sequence divergence. Slowly evolving proteins have been found to evolve slowly because of selection against toxic misfolding and misinteractions, linking their rate of evolution primarily to their abundance. Similarly, most slowly evolving sites in proteins are not directly involved in function, but mutating them has large impacts on protein structure and stability. Here, we review the studies of the emergent field of biophysical protein evolution that have shaped our current understanding of sequence divergence patterns. We also propose future research directions to develop this nascent field. äBiophysical models of protein evolution: Understanding the patterns of(epmc).pdf DeepDyve Pubget Overpricing