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10.1039/b817980h http://scihub22266oqcxt.onion/10.1039/b817980h C5962266!5962266 !19343235     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=19343235 &cmd=llinks): Failed to open stream: HTTP request failed! 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Structure-function relationships in peptoids: recent advances toward deciphering the structural requirements for biological function |pdf=|usr=}}{{19343235 }} gab.com Text Structure-function relationships in peptoids: recent advances toward deciphering the structural requirements for biological function JO: Org Biomol Chem http://www.kidney.de/pget.php?&tw=1&pmid=19343235 #FOAvip Oligomers of N-substituted glycine, or peptoids, are versatile tools to probe biological processes and hold promise as therapeutic agents. An underlying theme in the majority of recent peptoid research is the connection between peptoid function and peptoid structure. For certain applications, well-folded peptoids are essential for activity, while unstructured peptoids appear to suffice, or even are superior, for other applications. Currently, these structure-function connections are largely made after the design, synthesis, and characterization process. However, as guidelines for peptoid folding are elucidated and the known biological activities are expanded, we anticipate these connections will provide a pathway toward the de novo design of functional peptoids. In this perspective, we review several of the peptoid structure-function relationships that have been delineated over the past five years. Twit Text FOAVip Structure-function relationships in peptoids: recent advances toward deciphering the structural requirements for biological function ????Org Biomol Chem http://www.kidney.de/pget.php?&tw=1&pmid=19343235 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=19343235 #FOAvip English Wikipedia <ref>{{Cite pmid|19343235 }}</ref> Structure-function relationships in peptoids: recent advances toward deciphering the structural requirements for biological function #MMPMID19343235 Fowler SA ; Blackwell HE Org Biomol Chem 2009[Apr]; 7 (8 ): 1508-24 PMID19343235 show ga Oligomers of N-substituted glycine, or peptoids, are versatile tools to probe biological processes and hold promise as therapeutic agents. An underlying theme in the majority of recent peptoid research is the connection between peptoid function and peptoid structure. For certain applications, well-folded peptoids are essential for activity, while unstructured peptoids appear to suffice, or even are superior, for other applications. Currently, these structure-function connections are largely made after the design, synthesis, and characterization process. However, as guidelines for peptoid folding are elucidated and the known biological activities are expanded, we anticipate these connections will provide a pathway toward the de novo design of functional peptoids. In this perspective, we review several of the peptoid structure-function relationships that have been delineated over the past five years. |*Structure-Activity Relationship [MESH] |Amino Acid Sequence [MESH] |Amyloid/chemistry [MESH] |Anti-Infective Agents/chemistry [MESH] |Biomimetics [MESH] |Glycine/chemical synthesis/*chemistry/metabolism [MESH] |Islet Amyloid Polypeptide [MESH] |Molecular Sequence Data [MESH] |Peptoids/chemical synthesis/*chemistry/metabolism [MESH] |Protein Binding [MESH] |Protein Conformation [MESH] |Protein Folding [MESH]Structure-function relationships in peptoids: recent advances toward d(epmc).pdf DeepDyve Pubget Overpricing