1 40 1 Text A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text. URL Address <a href="http://doi.org/10.1021/jm070577s" target="_blank" rel="noreferrer noopener">http://doi.org/10.1021/jm070577s</a> Rights Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s). Pages 6501-6506 Issue 26 Volume 50 Search for Full-text Locate full-text within NEOMED Library's e-journal collections <p>Users with a NEOMED Library login can search for full-text journal articles at the following url: <a href="https://libraryguides.neomed.edu/home">https://libraryguides.neomed.edu/home</a></p> Dublin Core The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/. Title A name given to the resource Conformational comparisons of a series of tachykinin peptide analogs Publisher An entity responsible for making the resource available Journal of Medicinal Chemistry Date A point or period of time associated with an event in the lifecycle of the resource 2007 2007-12 Subject The topic of the resource Pharmacology & Pharmacy; escherichia-coli; nmr; dynamics; nuclear-magnetic-resonance; substance-p receptor; agonists; neuropeptides; bradykinin; molecular modeling investigations; sds micelles Creator An entity primarily responsible for making the resource Beard D J; Perrine S A; Phillips E; Hoque S; Conerly S; Tichenor C; Simmons M A; Young J K Description An account of the resource Previous studies have shown differences in the biological activity and the structure of two naturally occurring tachykinin peptides, substance P (SP, RPKPQQFFGLM-NH2),and ranatachykinin C (RTKC, HNPASFIGLM-NH2). To further understand the basis for these differences, four analogs that selectively incorporate the amino acid differences between SP and RTKC have been synthesized for study. The four peptide analogs studied have the following amino acid sequences: SP2-11, also known as des-Arg SP (PKPQQFFGLM-NH2); Q5A-SP (RPKPAQFFGLM-NH2); Q6S-SP (RPKPQSFFGLM-NH2); and Q5AQ6S-SP (RPKPASFFGLM-NH2). Nuclear magnetic resonance spectroscopy and molecular modeling calculations were performed on SP, RTKC, SP2-11, Q5A-SP, Q6S-SP, and Q5AQ6S-SP to compare their conformational differences and similarities in the presence of the membrane mimetic system sodium dodecyl sulfate. The molecular modeling data of the analogs Q5A-SP and Q6S-SP show residues 1-3 have a random conformation and residues 4-8 have a helical structure, while the C-terminus contains a poly C-7 conformation that is similar to SP but different from RTKC., The molecular modeling data of the analogs SP2-11 and Q5AQ6S-SP show a continuous helix conformation for residues 4-11 at the C-terminus, which is different from SP but similar to RTKC. These structural differences are related to the functional differences of binding of the peptides at the SP receptor (NK1). Identifier An unambiguous reference to the resource within a given context <a href="http://doi.org/10.1021/jm070577s" target="_blank" rel="noreferrer noopener">10.1021/jm070577s</a> Format The file format, physical medium, or dimensions of the resource Journal Article or Conference Abstract Publication 2007 agonists Beard D J bradykinin Conerly S dynamics escherichia-coli Hoque S Journal Article or Conference Abstract Publication Journal of medicinal chemistry molecular modeling investigations neuropeptides nmr nuclear-magnetic-resonance Perrine S A Pharmacology & Pharmacy Phillips E sds micelles Simmons M A substance-p receptor Tichenor C Young J K