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10.3390/ijms160923094 http://scihub22266oqcxt.onion/10.3390/ijms160923094 C4613353!4613353 !26404267     free     free     free Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26404267 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Int+J+Mol+Sci 2015 ; 16 (9 ): 23094-110 Nephropedia Template TP {{tp|p=26404267 |t=2015. Rational Protein Engineering Guided by Deep Mutational Scanning |pdf=|usr=}}{{26404267 }} gab.com Text Rational Protein Engineering Guided by Deep Mutational Scanning JO: Int J Mol Sci http://www.kidney.de/pget.php?&tw=1&pmid=26404267 #FOAvip Sequence-function relationship in a protein is commonly determined by the three-dimensional protein structure followed by various biochemical experiments. However, with the explosive increase in the number of genome sequences, facilitated by recent advances in sequencing technology, the gap between protein sequences available and three-dimensional structures is rapidly widening. A recently developed method termed deep mutational scanning explores the functional phenotype of thousands of mutants via massive sequencing. Coupled with a highly efficient screening system, this approach assesses the phenotypic changes made by the substitution of each amino acid sequence that constitutes a protein. Such an informational resource provides the functional role of each amino acid sequence, thereby providing sufficient rationale for selecting target residues for protein engineering. Here, we discuss the current applications of deep mutational scanning and consider experimental design. Twit Text FOAVip Rational Protein Engineering Guided by Deep Mutational Scanning ????Int J Mol Sci http://www.kidney.de/pget.php?&tw=1&pmid=26404267 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26404267 #FOAvip English Wikipedia <ref>{{Cite pmid|26404267 }}</ref> Rational Protein Engineering Guided by Deep Mutational Scanning #MMPMID26404267 Shin H ; Cho BK Int J Mol Sci 2015[Sep]; 16 (9 ): 23094-110 PMID26404267 show ga Sequence-function relationship in a protein is commonly determined by the three-dimensional protein structure followed by various biochemical experiments. However, with the explosive increase in the number of genome sequences, facilitated by recent advances in sequencing technology, the gap between protein sequences available and three-dimensional structures is rapidly widening. A recently developed method termed deep mutational scanning explores the functional phenotype of thousands of mutants via massive sequencing. Coupled with a highly efficient screening system, this approach assesses the phenotypic changes made by the substitution of each amino acid sequence that constitutes a protein. Such an informational resource provides the functional role of each amino acid sequence, thereby providing sufficient rationale for selecting target residues for protein engineering. Here, we discuss the current applications of deep mutational scanning and consider experimental design. |Amino Acid Sequence [MESH] |Animals [MESH] |DNA Mutational Analysis/*methods [MESH] |High-Throughput Nucleotide Sequencing/*methods [MESH] |Humans [MESH] |Molecular Sequence Data [MESH] |Mutagenesis [MESH] |Mutation [MESH] |Protein Engineering/*methods [MESH]Rational Protein Engineering Guided by Deep Mutational Scanning (epmc).pdf DeepDyve Pubget Overpricing