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10.1186/s13062-018-0209-6 http://scihub22266oqcxt.onion/10.1186/s13062-018-0209-6 C5960202!5960202!29776380     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       Biol+Direct 2018 ; 13 (ä): ä Nephropedia Template TP {{tp|p=29776380|t=2018. Use of designed sequences in protein structure recognition |pdf=|usr=}}{{29776380}} gab.com Text Use of designed sequences in protein structure recognition JO: Biol Direct http://www.kidney.de/pget.php?&tw=1&pmid=29776380 #FOAvip Background: Knowledge of the protein structure is a pre-requisite for improved understanding of molecular function. The gap in the sequence-structure space has increased in the post-genomic era. Grouping related protein sequences into families can aid in narrowing the gap. In the Pfam database, structure description is provided for part or full-length proteins of 7726 families. For the remaining 52% of the families, information on 3-D structure is not yet available. We use the computationally designed sequences that are intermediately related to two protein domain families, which are already known to share the same fold. These strategically designed sequences enable detection of distant relationships and here, we have employed them for the purpose of structure recognition of protein families of yet unknown structure. Results: We first measured the success rate of our approach using a dataset of protein families of known fold and achieved a success rate of 88%. Next, for 1392 families of yet unknown structure, we made structural assignments for part/full length of the proteins. Fold association for 423 domains of unknown function (DUFs) are provided as a step towards functional annotation. Conclusion: The results indicate that knowledge-based filling of gaps in protein sequence space is a lucrative approach for structure recognition. Such sequences assist in traversal through protein sequence space and effectively function as ?linkers?, where natural linkers between distant proteins are unavailable. Reviewers: This article was reviewed by Oliviero Carugo, Christine Orengo and Srikrishna Subramanian. Electronic supplementary material: The online version of this article (10.1186/s13062-018-0209-6) contains supplementary material, which is available to authorized users. Twit Text FOAVip Use of designed sequences in protein structure recognition ????Biol Direct http://www.kidney.de/pget.php?&tw=1&pmid=29776380 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29776380 #FOAvip English Wikipedia <ref>{{Cite pmid|29776380}}</ref> Use of designed sequences in protein structure recognition #MMPMID29776380 Kumar G; Mudgal R; Srinivasan N; Sandhya S Biol Direct 2018[]; 13 (ä): ä PMID29776380show ga Background: Knowledge of the protein structure is a pre-requisite for improved understanding of molecular function. The gap in the sequence-structure space has increased in the post-genomic era. Grouping related protein sequences into families can aid in narrowing the gap. In the Pfam database, structure description is provided for part or full-length proteins of 7726 families. For the remaining 52% of the families, information on 3-D structure is not yet available. We use the computationally designed sequences that are intermediately related to two protein domain families, which are already known to share the same fold. These strategically designed sequences enable detection of distant relationships and here, we have employed them for the purpose of structure recognition of protein families of yet unknown structure. Results: We first measured the success rate of our approach using a dataset of protein families of known fold and achieved a success rate of 88%. Next, for 1392 families of yet unknown structure, we made structural assignments for part/full length of the proteins. Fold association for 423 domains of unknown function (DUFs) are provided as a step towards functional annotation. Conclusion: The results indicate that knowledge-based filling of gaps in protein sequence space is a lucrative approach for structure recognition. Such sequences assist in traversal through protein sequence space and effectively function as ?linkers?, where natural linkers between distant proteins are unavailable. Reviewers: This article was reviewed by Oliviero Carugo, Christine Orengo and Srikrishna Subramanian. Electronic supplementary material: The online version of this article (10.1186/s13062-018-0209-6) contains supplementary material, which is available to authorized users. äUse of designed sequences in protein structure recognition (epmc).pdf DeepDyve Pubget Overpricing