Membrane-induced secondary structures of neuropeptides: A comparison of the solution conformations adopted by agonists and antagonists of the mammalian tachykinin NK₁ receptor

Keyphrases

• Secondary Structure 100%
• Solution Conformation 100%
• N-terminus 100%
• Arginase-1 (Arg-1) 100%
• Sodium Dodecyl Sulfate 100%
• C-terminus 100%
• NK1 Receptor 100%
• Neurokinin B 100%
• Neuropeptides 100%
• Membrane Model 100%
• Tachykinin NK1 Receptor 100%
• Turn Structure 100%
• Well-defined 50%
• Selective Antagonist 50%
• Binding Assay 50%
• Biologically Active 50%
• Biological Activity 50%
• Selective Agonist 50%
• Simulated Annealing 50%
• Helical Structures 50%
• In Vitro Condition 50%
• Analogue Study 50%
• G-coupled Protein Receptors 50%
• Membrane Interface 50%
• Modeling Packages 50%
• Nuclear Overhauser Effect 50%
• NMR Chemical Shift Assignments 50%
• 1H NMR Chemical Shifts 50%
• Micelle System 50%
• Rough Approximation 50%
• Model Matrix 50%
• Ligand Conformation 50%
• Model Environment 50%
• Binding Potency 50%
• Conformational Study 50%
• Interface Environment 50%
• Two-dimensional NMR 50%
• Molecular Dynamics 50%
• NMR Techniques 50%
• Three Dimensional Structure 50%
• Dynamic Annealing 50%
• Conformational Differences 50%
• Proton Resonances 50%
• Induced Structure 50%

Chemistry

• Secondary Structure 100%
• Sodium Dodecyl Sulfate 100%
• Neuropeptide 100%
• Tachykinin 100%
• Micelle 100%
• Bioactivity 50%
• Molecular Dynamics 50%
• Two-Dimensional NMR 50%
• 1H NMR Spectroscopy 50%
• Helical Structure 50%
• Tachykinin Receptor Agonist 50%
• Nuclear Overhauser Effect 50%
• Chemical Shift 50%
• Peptide 50%