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10.1002/pro.2209 http://scihub22266oqcxt.onion/10.1002/pro.2209 23238853!3595458!23238853     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Protein+Sci 2013 ; 22 (3): 280-6 Nephropedia Template TP {{tp|p=23238853|t=2013. Evidences for the unfolding mechanism of three-dimensional domain swapping |pdf=|usr=}}{{23238853}} gab.com Text Evidences for the unfolding mechanism of three-dimensional domain swapping JO: Protein Sci http://www.kidney.de/pget.php?&tw=1&pmid=23238853 #FOAvip The full or partial unfolding of proteins is widely believed to play an essential role in three-dimensional domain swapping. However, there is little research that has rigorously evaluated the association between domain swapping and protein folding/unfolding. Here, we examined a kinetic model in which domain swapping occurred via the denatured state produced by the complete unfolding of proteins. The relationships between swapping kinetics and folding/unfolding thermodynamics were established, which were further adopted as criteria to show that the proposed mechanism dominates in three representative proteins: Cyanovirin-N (CV-N), the C-terminal domain of SARS-CoV main protease (M(pro)-C), and a single mutant of oxidized thioredoxin (Trx_W28A(ox)). Twit Text FOAVip Evidences for the unfolding mechanism of three-dimensional domain swapping ????Protein Sci http://www.kidney.de/pget.php?&tw=1&pmid=23238853 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=23238853 #FOAvip English Wikipedia <ref>{{Cite pmid|23238853}}</ref> Evidences for the unfolding mechanism of three-dimensional domain swapping #MMPMID23238853 Liu Z; Huang Y Protein Sci 2013[Mar]; 22 (3): 280-6 PMID23238853show ga The full or partial unfolding of proteins is widely believed to play an essential role in three-dimensional domain swapping. However, there is little research that has rigorously evaluated the association between domain swapping and protein folding/unfolding. Here, we examined a kinetic model in which domain swapping occurred via the denatured state produced by the complete unfolding of proteins. The relationships between swapping kinetics and folding/unfolding thermodynamics were established, which were further adopted as criteria to show that the proposed mechanism dominates in three representative proteins: Cyanovirin-N (CV-N), the C-terminal domain of SARS-CoV main protease (M(pro)-C), and a single mutant of oxidized thioredoxin (Trx_W28A(ox)). |*Models, Molecular[MESH] |Algal Proteins/*chemistry/genetics/metabolism[MESH] |Amino Acid Substitution[MESH] |Bacterial Proteins/*chemistry/genetics/metabolism[MESH] |Carrier Proteins/*chemistry/genetics/metabolism[MESH] |Coronavirus 3C Proteases[MESH] |Cysteine Endopeptidases/*chemistry/genetics/metabolism[MESH] |Dimerization[MESH] |Kinetics[MESH] |Mutant Proteins/*chemistry/genetics/metabolism[MESH] |Oxidation-Reduction[MESH] |Peptide Fragments/*chemistry/genetics/metabolism[MESH] |Protein Denaturation[MESH] |Protein Refolding[MESH] |Protein Structure, Tertiary[MESH] |Protein Unfolding[MESH] |Recombinant Proteins/chemistry/metabolism[MESH] |Thermodynamics[MESH] |Thioredoxins/*chemistry/genetics/metabolism[MESH]Evidences for the unfolding mechanism of three-dimensional domain swap(epmc).pdf DeepDyve Pubget Overpricing