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10.1016/j.jmb.2021.167325 http://scihub22266oqcxt.onion/10.1016/j.jmb.2021.167325 34695380!ä!34695380 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       J+Mol+Biol 2021 ; 433 (24): 167325 Nephropedia Template TP {{tp|p=34695380|t=2021. Folding Intermediates, Heterogeneous Native Ensembles and Protein Function |pdf=|usr=}}{{34695380}} gab.com Text Folding Intermediates, Heterogeneous Native Ensembles and Protein Function JO: J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=34695380 #FOAvip Single domain proteins fold via diverse mechanisms emphasizing the intricate relationship between energetics and structure, which is a direct consequence of functional constraints and demands imposed at the level of sequence. On the other hand, elucidating the interplay between folding mechanisms and function is challenging in large proteins, given the inherent shortcomings in identifying metastable states experimentally and the sampling limitations associated with computational methods. Here, we show that free energy profiles and surfaces of large systems (>150 residues), as predicted by a statistical mechanical model, display a wide array of folding mechanisms with ubiquitous folding intermediates and heterogeneous native ensembles. Importantly, residues around the ligand binding or enzyme active site display a larger tendency to partially unfold and this manifests as intermediates or excited states along the folding coordinate in ligand binding domains, transcription repressors, and representative enzymes from all the six classes, including the SARS-CoV-2 receptor binding domain (RBD) of the spike protein and the protease M(pro). It thus appears that it is relatively easier to distill the imprints of function on the folding landscape of larger proteins as opposed to smaller systems. We discuss how an understanding of energetic-entropic features in ordered proteins can pinpoint specific avenues through which folding mechanisms, populations of partially structured states and function can be engineered. Twit Text FOAVip Folding Intermediates, Heterogeneous Native Ensembles and Protein Function ????J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=34695380 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34695380 #FOAvip English Wikipedia <ref>{{Cite pmid|34695380}}</ref> Folding Intermediates, Heterogeneous Native Ensembles and Protein Function #MMPMID34695380 Naganathan AN; Dani R; Gopi S; Aranganathan A; Narayan A J Mol Biol 2021[Dec]; 433 (24): 167325 PMID34695380show ga Single domain proteins fold via diverse mechanisms emphasizing the intricate relationship between energetics and structure, which is a direct consequence of functional constraints and demands imposed at the level of sequence. On the other hand, elucidating the interplay between folding mechanisms and function is challenging in large proteins, given the inherent shortcomings in identifying metastable states experimentally and the sampling limitations associated with computational methods. Here, we show that free energy profiles and surfaces of large systems (>150 residues), as predicted by a statistical mechanical model, display a wide array of folding mechanisms with ubiquitous folding intermediates and heterogeneous native ensembles. Importantly, residues around the ligand binding or enzyme active site display a larger tendency to partially unfold and this manifests as intermediates or excited states along the folding coordinate in ligand binding domains, transcription repressors, and representative enzymes from all the six classes, including the SARS-CoV-2 receptor binding domain (RBD) of the spike protein and the protease M(pro). It thus appears that it is relatively easier to distill the imprints of function on the folding landscape of larger proteins as opposed to smaller systems. We discuss how an understanding of energetic-entropic features in ordered proteins can pinpoint specific avenues through which folding mechanisms, populations of partially structured states and function can be engineered. |*Models, Molecular[MESH] |*Protein Conformation[MESH] |*Protein Folding[MESH] |Enzymes/*chemistry/*metabolism[MESH] |Humans[MESH] |Protein Binding[MESH] |Protein Domains[MESH]Folding Intermediates, Heterogeneous Native Ensembles and Protein Func(epmc).pdf DeepDyve Pubget Overpricing