John K. Young
Mississippi State University
14 Papers
97 Citations
John K. Young is an academic researcher from Mississippi State University. The author has contributed to research in topics: Haloferax volcanii & Nuclear magnetic resonance spectroscopy. The author has an hindex of 9, co-authored 14 publications.
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Papers
NMR and molecular modeling investigations of the neuropeptide substance P in the presence of 15 mM sodium dodecyl sulfate micelles
TL;DR: Two‐dimensional nmr spectroscopy experiments and simulated annealing calculations were used to investigate the conformation adopted in the presence of the membrane model system sodium dodecyl sulfate and yielded a structure that is consistent with the model of a neurokinin‐1 selective ligand proposed by Convert.
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Membrane-induced secondary structures of neuropeptides: a comparison of the solution conformations adopted by agonists and antagonists of the mammalian tachykinin NK1 receptor.
TL;DR: What is believed to be the first documented example of an inducement of distinctly different secondary structure types onto agonists and antagonists selective for the same G-coupled protein receptor using the same membrane-model matrix is presented.
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Nmr and molecular modeling investigations of the neuropeptide bradykinin in three different solvent systems: DMSO, 9 : 1 dioxane/water, and in the presence of 7.4 mM lyso phosphatidylcholine micelles
John K. Young,Rickey P. Hicks +1 more
TL;DR: The results suggest that the β‐turn at the C‐terminus of bradykinin is an important secondary structural feature for receptor recognition and binding.
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The interactions of neuropeptides with membrane model systems: a case study.
TL;DR: The interaction between SP and BK with LPC based on nmr results are characterized as extrinsic, with the interaction between ME and SDS characterized as weakly intrinsic.
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The use of UV-visible spectroscopy for the determination of hydrophobic interactions between neuropeptides and membrane model systems.
TL;DR: The aromatic residues of substance P, bradykinin, and Des‐Arg9 bradykinsin all exhibited the 1−nm bathochromic shift in the presence of sodium dodecyl sulfate while those of Met‐enkephalin did not, and the opposite effects were observed in the absence of lysophosphatidylcholine micelles.
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